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nasF nasF rimI rimI hmoA hmoA yfiQ yfiQ yfhH yfhH gsaB gsaB ygzB ygzB ygaN ygaN hemZ hemZ yhaR yhaR yhaA yhaA yhfA yhfA yhgB yhgB hmoB hmoB hemE hemE hemH hemH hemY hemY yjcF yjcF yjcG yjcG yjcH yjcH ctaO ctaO yjjA yjjA ykkB ykkB ylaH ylaH ylaL ylaL ctaA ctaA ctaB ctaB ctaC ctaC ctaD ctaD ctaE ctaE ctaF ctaF ctaG ctaG ylbA ylbA ymfC ymfC yneK yneK yozB yozB scuA scuA ypzF ypzF ypbS ypbS dynA dynA qcrC qcrC qcrB qcrB qcrA qcrA ypiF ypiF resE resE resD resD resC resC resB resB resA resA yqzF yqzF yqgY yqgY cccA cccA hemN hemN lepA lepA hemL hemL hemB hemB hemD hemD hemC hemC hemX hemX hemA hemA ysxD ysxD acuA acuA acuB acuB acuC acuC ytkA ytkA yugN yugN yugM yugM kapD kapD yuxK yuxK yuiB yuiB yuiA yuiA yutF yutF yutE yutE yutD yutD yutC yutC cccB cccB ywpJ ywpJ glcR glcR ywpG ywpG ywpF ywpF ywjG ywjG ywhD ywhD ywhC ywhC ywhB ywhB hemQ hemQ qoxD qoxD qoxC qoxC qoxB qoxB qoxA qoxA ywcB ywcB ywcA ywcA yybF yybF yybE yybE yybD yybD yybC yybC
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
nasFuroporphyrin-III C-methyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the precorrin methyltransferase family. (483 aa)
rimIRibosomal protein S18 alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18. (151 aa)
hmoAHeme-degrading monooxygenase; Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. (108 aa)
yfiQPutative membrane component involved in biofilm formation; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (362 aa)
yfhHConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (104 aa)
gsaBGlutamate-1-semialdehyde aminotransferase, class III aminotransferase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (429 aa)
ygzBPutative membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (117 aa)
ygaNPutative sulfur-related oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (178 aa)
hemZCoproporphyrinogen III oxidase; Involved in the biosynthesis of porphyrin-containing compound; Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemZ subfamily. (501 aa)
yhaRPutative dehydratase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (255 aa)
yhaAPutative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (396 aa)
yhfAPutative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (463 aa)
yhgBHypothetical protein; Evidence 5: No homology to any previously reported sequences. (104 aa)
hmoBHeme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. (166 aa)
hemEUroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (353 aa)
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. (310 aa)
hemYProtoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. (470 aa)
yjcFPutative 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. (140 aa)
yjcGPutative RNA ligase or phosphoesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (171 aa)
yjcHPutative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (240 aa)
ctaOMinor protoheme IX farnesyltransferase 1 (heme O synthase); 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. (329 aa)
yjjAPutative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (270 aa)
ykkBPutative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (172 aa)
ylaHConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (105 aa)
ylaLConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (161 aa)
ctaAheme-A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation. (306 aa)
ctaBProtoheme IX farnesyltransferase 2; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (305 aa)
ctaCCytochrome caa3 oxidase (subunit II); Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (356 aa)
ctaDCytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. (622 aa)
ctaECytochrome caa3 oxidase (subunit III); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase subunit 3 family. (207 aa)
ctaFCytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. (110 aa)
ctaGCytochrome aa(3) assembly factor; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor. (297 aa)
ylbAConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (120 aa)
ymfCPutative transcriptional regulator (GntR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. (241 aa)
yneKConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (142 aa)
yozBPutative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (178 aa)
scuAAssembly factor BSco of the Cu(A) site of cytochrome c oxidase; Necessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling; Belongs to the SCO1/2 family. (193 aa)
ypzFHypothetical protein; Evidence 5: No homology to any previously reported sequences. (48 aa)
ypbSConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (85 aa)
dynADynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (1193 aa)
qcrCMenaquinol:cytochrome c oxidoreductase (cytochrome cc subunit); Component of the menaquinol-cytochrome c reductase complex. (255 aa)
qcrBMenaquinol:cytochrome c oxidoreductase (cytochrome b subunit); Component of the menaquinol-cytochrome c reductase complex. (224 aa)
qcrAMenaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. (167 aa)
ypiFConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (148 aa)
resETwo-component sensor histidine kinase; Member of the two-component regulatory system ResD/ResE involved in the global regulation of aerobic and anaerobic respiration. Probably phosphorylates ResD. (589 aa)
resDTwo-component response regulator; Member of the two-component regulatory system ResD/ResE. Required for the expression of resA, ctaA, qcrABC and fnr; activation role in global regulation of aerobic and anaerobic respiration. (240 aa)
resCFactor required for cytochrome c synthesis; Required for the biogenesis of c-type cytochromes. (391 aa)
resBFactor required for cytochrome c synthesis; Required for the biogenesis of c-type cytochromes. (542 aa)
resAExtracytoplasmic thioredoxin involved in cytochrome c maturation (lipoprotein); Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation. Belongs to the thioredoxin family. ResA subfamily. (179 aa)
yqzFConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (78 aa)
yqgYConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (81 aa)
cccACytochrome c550; Not essential for growth on minimal or rich media. (120 aa)
hemNCoproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine (By similarity). (379 aa)
lepARibosomal elongation factor, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. (612 aa)
hemLGlutamate-1-semialdehyde 2,1-aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (430 aa)
hemBDelta-aminolevulinic acid dehydratase (porphobilinogen synthase); Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). (324 aa)
hemDUroporphyrinogen III cosynthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Belongs to the uroporphyrinogen-III synthase family. (262 aa)
hemCPorphobilinogen deaminase (hydroxymethylbilane synthase); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (314 aa)
hemXNegative effector of the concentration of glutamyl-tRNA reductase HemA; Required for HemL synthesis; To M.leprae U1620K. (276 aa)
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (455 aa)
ysxDPutative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (165 aa)
acuAProtein acetyltransferase; Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue. (210 aa)
acuBComponent of the acetoin degradation regulation pathway; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source. (214 aa)
acuCProtein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. (387 aa)
ytkAPutative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type lp: lipoprotein. (145 aa)
yugNConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (134 aa)
yugMPutative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (123 aa)
kapDPutative exoribonuclease (3'-5'); Specifically inhibits the KinA pathway to sporulation. (205 aa)
yuxKConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the DCC thiol-disulfide oxidoreductase family. (137 aa)
yuiBConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (106 aa)
yuiAConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (47 aa)
yutFPutative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family. (256 aa)
yutEConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the UPF0331 family. (144 aa)
yutDConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12770717. (91 aa)
yutCPutative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type lp: lipoprotein. (210 aa)
cccBCytochrome c551; Electron carrier protein. (112 aa)
ywpJPutative phosphatase; Catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro (By similarity). To a lesser extent, dephosphorylates flavin mononucleotide (FMN) in vitro. (285 aa)
glcRTranscriptional regulator (DeoR family); Plays a role in carbon catabolite repression (CCR). Specifically required for transcriptional repression of the levanase operon by glucose but not by other sugars. (258 aa)
ywpGHypothetical protein; Evidence 5: No homology to any previously reported sequences. (127 aa)
ywpFConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (136 aa)
ywjGPutative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (173 aa)
ywhDConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (172 aa)
ywhCPutative metal-dependent hydrolase; 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 peptidase M50B family. (219 aa)
ywhB1,3-keto-enol tautomerase; Catalyzes both 1,3- and 1,5-keto-enol tautomerization of the diacid 2-hydroxymuconate (2-hydroxy-2,4-hexadienedioate) to produce 2- oxo-4-hexenedioate. This reaction is highly stereoselective and produces a mixture of stereoisomers, where the (3S)-isomer of 2-oxo-4- hexenedioate predominates. Also catalyzes the tautomerization of 2- hydroxymuconate to 2-oxo-3-hexenedioate, however this reaction is slower and occurs after the tautomerization of 2-hydroxymuconate to 2- oxo-4-hexenedioate. Using 2-hydroxy-2,4-pentadienoate, phenylenolpyruvate, (p-hydroxyphenyl)- [...] (62 aa)
hemQEssential component of heme biosynthesis; May function as heme-dependent peroxidase. (254 aa)
qoxDCytochrome aa3-600 quinol oxidase (subunit IV); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (124 aa)
qoxCCytochrome aa3-600 quinol oxidase (subunit III); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (204 aa)
qoxBCytochrome aa3-600 quinol oxidase (subunit I); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (649 aa)
qoxACytochrome aa3-600 quinol oxidase (subunit II); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I (By similarity). (321 aa)
ywcBPutative phage protein (superinfection immunity); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin. (102 aa)
ywcAPutative acetate Na+-dependent symporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (513 aa)
yybFPutative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (404 aa)
yybEPutative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the LysR transcriptional regulatory family. (292 aa)
yybDPutative acetyltransferase; Could catalyze the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. (147 aa)
yybCPutative integral membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (159 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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