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sodA sodA salA salA nagZ nagZ amiE amiE glmS glmS ydaP ydaP acoL acoL yitI yitI mecA mecA pdhD pdhD spoVD spoVD ftsZ ftsZ citB citB eglS eglS sodF sodF lpdV lpdV efp efp gcvPB gcvPB dnaK dnaK obg obg gapB gapB pyk pyk ald ald opuBD opuBD opuBB opuBB opuCD opuCD opuCB opuCB tpiA tpiA fbaA fbaA pyrG pyrG hutG hutG argI argI
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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experimentally determined
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sodASuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (202 aa)
salAMrp family regulator; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (352 aa)
nagZN-acetylglucosaminidase lipoprotein; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves muropeptides, but not peptidoglycan. Belongs to the glycosyl hydrolase 3 family. (642 aa)
amiEAmidase hydrolyzing N-acetylmuramyl-L-Ala bond of MurNAc peptides; Involved in muropeptide recycling. Hydrolyzes the amide bond between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the stem peptide. Cannot hydrolyze muropeptides containing N- acetylglucosamine (GlcNAc) at the non-reducing end. (441 aa)
glmSL-glutamine-D-fructose-6-phosphate amidotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (600 aa)
ydaPPutative enzyme with pyruvate as substrate; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (574 aa)
acoLAcetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (458 aa)
yitIPutative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the acetyltransferase family. (149 aa)
mecAAdaptor protein controlling oligomerization of the AAA+ protein ClpC; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC. (218 aa)
pdhDDihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa)
spoVDPenicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. (646 aa)
ftsZCell-division initiation protein; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. (382 aa)
citBAconitate hydratase (aconitase); Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the rehydration of 2- methyl-cis-aconitate to produce 2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the conce [...] (909 aa)
eglSEndo-1,4-beta-glucanase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (499 aa)
sodFSuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. (281 aa)
lpdVBranched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (474 aa)
efpElongation factor P; 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 (By similarity). (185 aa)
gcvPBGlycine decarboxylase (subunit 2) (glycine cleavage system protein P); 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 (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily. (488 aa)
dnaKMolecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (611 aa)
obgGTPase involved in cell partioning and DNA repair; Necessary for the transition from vegetative growth to stage 0 or stage II of sporulation, but sporulation subsequent to these stages is unaffected at 45 degrees Celsius. This ts effect is probably due solely to the E-79 mutation. Required for expression of early sporulation genes, further suggesting a role in the induction of sporulation. Depletion effects on sporulation can be partially suppressed by missense mutations in spo0A. Strains depleted for obg stop growing after about 3 hours and do not induce the sigma-B factor following e [...] (428 aa)
gapBGlyceraldehyde-3-phosphate dehydrogenase; Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3- bisphosphoglycerate (BPG) using the cofactor NADP. 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 NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG; Belongs to the gl [...] (340 aa)
pykPyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. (585 aa)
aldL-alanine dehydrogenase; Catalyzes the reversible oxidative deamination of L-alanine to pyruvate. This enzyme is a key factor in the assimilation of L- alanine as an energy source through the tricarboxylic acid cycle during sporulation. (378 aa)
opuBDCholine ABC transporter (permease); Involved in a high affinity multicomponent binding-protein- dependent transport system for choline; probably responsible for the translocation of the substrate across the membrane. (226 aa)
opuBBCholine ABC transporter (permease); Involved in a high affinity multicomponent binding-protein- dependent transport system for choline; probably responsible for the translocation of the substrate across the membrane. (217 aa)
opuCDGlycine betaine/carnitine/choline/choline sulfate ABC transporter (permease); Involved in a high affinity multicomponent binding-protein- dependent transport system for glycine betaine, carnitine and choline; probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. (229 aa)
opuCBGlycine betaine/carnitine/choline/choline sulfate ABC transporter (permease); Involved in a high affinity multicomponent binding-protein- dependent transport system for glycine betaine, carnitine and choline; probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily. (217 aa)
tpiATriose phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (253 aa)
fbaAFructose-1,6-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. (285 aa)
pyrGCTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (535 aa)
hutGFormiminoglutamate hydrolase; Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. (319 aa)
argIArginase; Involved in the catabolism of arginine. Belongs to the arginase family. (296 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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