SIMILARITY: Belongs to the TrpF family.


FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family.


SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.


SIMILARITY: Belongs to the UPF0102 family.


FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.


FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.


FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family.


FUNCTION: This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL22 family.


FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SIMILARITY: Belongs to the enolase family.


FUNCTION: With S5 and S12 plays an important role in translational accuracy. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS4 family.


FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. HutI family.


FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. SIMILARITY: Belongs to the UPF0677 family.


FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.


FUNCTION: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WzyE family.


FUNCTION: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily.


FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL11 family.


FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.


FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL23 family.


FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


SIMILARITY: Belongs to the WrbA family.


FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.


FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. SIMILARITY: Belongs to the universal ribosomal protein uL13 family.


FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase alpha chain family.


FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.


FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0761 family.


FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL10 family.


SUBCELLULAR LOCATION: Secreted.


FUNCTION: Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. SIMILARITY: Belongs to the Fmt family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family.


SIMILARITY: Belongs to the universal ribosomal protein uS9 family.


FUNCTION: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family.


FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family.


FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family.


FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.


FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.


SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB subfamily.


FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family.


FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.


FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.


FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.


FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family.


FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. FUNCTION: Forms part of the polypeptide exit tunnel. SIMILARITY: Belongs to the universal ribosomal protein uL4 family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family.


FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). SIMILARITY: Belongs to the LpxK family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. SIMILARITY: Belongs to the universal ribosomal protein uS7 family.


FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family.


FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.


FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). SIMILARITY: Belongs to the shikimate dehydrogenase family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. SIMILARITY: Belongs to the HrcA family.


FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. SIMILARITY: Belongs to the RNase PH family.


FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family.


FUNCTION: Involved in the binding of tRNA to the ribosomes. SIMILARITY: Belongs to the universal ribosomal protein uS10 family.


FUNCTION: Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.


FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.


FUNCTION: NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmG family.


FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.


SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family.


SIMILARITY: Belongs to the UPF0234 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the fosfomycin resistance protein family. FosB subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family.


FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). SIMILARITY: Belongs to the IPP transferase family.


FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family.


FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family.


FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. SIMILARITY: Belongs to the IspG family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family.


FUNCTION: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endoribonuclease YbeY family.


FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. SIMILARITY: Belongs to the calmodulin family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family.


FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family.


FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily.


FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family.


FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvB family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family.


FUNCTION: Methylates ribosomal protein L11. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.


FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GrpE family.


FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family.


FUNCTION: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family.


FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family.


SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family.


FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uS19 family.


FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. SIMILARITY: Belongs to the AP endonuclease 2 family.


FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.


FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the chaperonin (HSP60) family.


FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. SIMILARITY: Belongs to the thymidylate kinase family.


SIMILARITY: Belongs to the universal ribosomal protein uL30 family.


FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. SIMILARITY: Belongs to the universal ribosomal protein uL16 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease gamma subunit family.


FUNCTION: Multidrug efflux pump that functions probably as a Na(+)/drug antiporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family. MdtK subfamily.


FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD kinase family.


FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). SIMILARITY: Belongs to the glutamyl-tRNA reductase family.


FUNCTION: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell- pathogen interactions. Catalyzes the conversion of CMP-N- acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.


FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). SIMILARITY: Belongs to the amidase family. GatA subfamily.


FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. SIMILARITY: Belongs to the ClpX chaperone family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family.


FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. SIMILARITY: Belongs to the chorismate synthase family.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.


FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric- sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.


FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.


SIMILARITY: Belongs to the universal ribosomal protein uS2 family.


FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. SIMILARITY: Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. SIMILARITY: Belongs to the glutaminase PdxT/SNO family.


FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.


FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family.


FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family.


FUNCTION: Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans- translation. SUBCELLULAR LOCATION: Cytoplasm Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. SIMILARITY: Belongs to the SmpB family.


FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. SIMILARITY: Belongs to the dUTPase family.


FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase family.


FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. SIMILARITY: Belongs to the DMRL synthase family.


FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family.


FUNCTION: Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family.


FUNCTION: May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. SIMILARITY: Belongs to the RecR family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family.


FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.


FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.


FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.


FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.


FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP). SIMILARITY: Belongs to the DXR family.


FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL23 family.


FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.


FUNCTION: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YqgF nuclease family.


FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family.


FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family.


FUNCTION: Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. SIMILARITY: Belongs to the Fe(2+)-trafficking protein family.


FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. SIMILARITY: Belongs to the type IA topoisomerase family.


FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP). SIMILARITY: Belongs to the transketolase family. DXPS subfamily.


FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FGAMS family.


FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.


FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvA family.


FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase family.


FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily.


FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with the membrane possibly through PlsY. SIMILARITY: Belongs to the PlsX family.


FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site- terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Mitochondrion Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.


FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.


FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.


FUNCTION: This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. SIMILARITY: Belongs to the universal ribosomal protein uL18 family.


FUNCTION: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.


FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.


FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.


FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily.


SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO small chain family.


SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.


FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. SIMILARITY: Belongs to the Hfq family.


SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.


FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily.


FUNCTION: Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.


FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.


SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family.


FUNCTION: Seems to play a role in the dimerization of PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbT family.


FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EF-Ts family.


FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily.


FUNCTION: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family.


FUNCTION: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DNA polymerase type-Y family.


FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiG family.


FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family.


FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiI family.


FUNCTION: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRF family.


SUBCELLULAR LOCATION: Plastid, chloroplast.


FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urocanase family.


SIMILARITY: Belongs to the SAICAR synthetase family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family.


FUNCTION: One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL2 family.


FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.


FUNCTION: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.


FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.


FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.


SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the FliE family.


FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine). SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.


FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). SIMILARITY: Belongs to the succinylarginine dihydrolase family.


FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.


FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.


FUNCTION: Has a role in the initiation of DNA replication. Required at S-phase checkpoint (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the SLD2 family.


FUNCTION: Plays a major role in protein secretion by helping the post- translocational extracellular folding of several secreted proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the PrsA family.


FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family.


FUNCTION: Catalyzes the synthesis of GMP from XMP.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdpA family.


FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MobA family.


FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family.


FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family.


FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Note=Relocalizes to mitochondria after H(2)O(2) exposure. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family.


FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose isomerase family.


FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. SIMILARITY: Belongs to the TrpA family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family.


FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. SIMILARITY: Belongs to the polypeptide deformylase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.


FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL14 family.


FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.


FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single- stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvC family.


FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family.


SIMILARITY: Belongs to the UPF0301 (AlgH) family.


SIMILARITY: Belongs to the UPF0246 family.


FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. SIMILARITY: Belongs to the histidinol dehydrogenase family.


FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.


FUNCTION: Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.


SIMILARITY: Belongs to the SfsA family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily.


FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A8 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IF-1 family.


FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.


FUNCTION: This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. SIMILARITY: Belongs to the universal ribosomal protein uL6 family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family.


FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family.


FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.


FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.


FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.


FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family.


FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the QueA family.


SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamate 5-kinase family.


FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family.


FUNCTION: Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the YbaB/EbfC family.


SIMILARITY: Belongs to the UPF0265 family.


FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. SIMILARITY: Belongs to the HAM1 NTPase family.


FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family.


FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. SIMILARITY: Belongs to the ThiD family.


FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit beta family.


FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. SIMILARITY: Belongs to the FGGY kinase family.


FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD subfamily.


FUNCTION: Binds together with bS18 to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family.


FUNCTION: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the L/F-transferase family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family.


FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase RlmH family.


FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. SIMILARITY: Belongs to the PyrI family.


FUNCTION: The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecF family.


FUNCTION: Cleaves the N-terminal amino acid of tripeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20B family.


FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the betacoronaviruses M protein family.


FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. SIMILARITY: Belongs to the universal ribosomal protein uS14 family.


FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family.


FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.


FUNCTION: Stimulates gene expression driven by the HIV-2 LTR. Prevents infected cells from undergoing mitosis and proliferating, by inducing arrest or delay in the G2 phase of the cell cycle. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus.


FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diaminopimelate epimerase family.


FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.


FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1- E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E1 protein family.


FUNCTION: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the IF-1 family.


FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SIMILARITY: Belongs to the beta/gamma-crystallin family.


FUNCTION: Involved in resistance toward heavy metals. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutA family.


SIMILARITY: Belongs to the CinA family.


FUNCTION: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. SIMILARITY: Belongs to the peptidase S24 family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 family.


FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily.


FUNCTION: This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.


FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabZ subfamily.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.


FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.


FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. SIMILARITY: Belongs to the aldehyde dehydrogenase family.


FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsB family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family.


FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscL family.


FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. SIMILARITY: Belongs to the DHBP synthase family.


FUNCTION: Could be involved in insertion of integral membrane proteins into the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the UPF0161 family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uS15 family.


FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SIMILARITY: Belongs to the HMBS family.


FUNCTION: Required for insertion of 4Fe-4S clusters for at least IspG. SIMILARITY: Belongs to the HesB/IscA family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease beta subunit family.


SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.


FUNCTION: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. SIMILARITY: Belongs to the CheD family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to mid-cell in an FtsZ-dependent manner. SIMILARITY: Belongs to the ZapD family.


FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family.


FUNCTION: With S4 and S5 plays an important role in translational accuracy. FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS12 family.


FUNCTION: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein Note=Localizes to the Z ring in an FtsZ-dependent manner. SIMILARITY: Belongs to the ZipA family.


FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family.


FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbH family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.


FUNCTION: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PNP synthase family.


SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family.


FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.


FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase E subunit family.


FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.


FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SIMILARITY: Belongs to the LpxB family.


SIMILARITY: Belongs to the polysaccharide lyase 1 family.


FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. SIMILARITY: Belongs to the bacterial histone-like protein family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SIMILARITY: Belongs to the universal ribosomal protein uL3 family.


FUNCTION: Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.


SIMILARITY: Belongs to the glutaminase family.


FUNCTION: Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.


FUNCTION: This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. SIMILARITY: Belongs to the DNA mismatch repair MutS family.


FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PTH family.


FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5- hydroxymethylpyrimidine phosphate (HMP-P). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.


FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoaE family.


FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. SIMILARITY: Belongs to the universal ribosomal protein uS13 family.


FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG subfamily.


FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. SIMILARITY: Belongs to the MinE family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.


FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccA family.


FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family.


FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).


FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily.


FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family.


FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the oligoribonuclease family.


FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily.


SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KAE1 / TsaD family.


FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family.


FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala- tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.


FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NDK family.


FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatC family.


FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.


FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family.


FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family.


FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. SIMILARITY: Belongs to the UPRTase family.


FUNCTION: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family.


FUNCTION: Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.


SIMILARITY: Belongs to the PurH family.


FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.


FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. SIMILARITY: Belongs to the ThiC family.


FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaJ family.