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ptb ptb mmgB mmgB gabD gabD abh abh gabT gabT nasD nasD nasE nasE spoIIE spoIIE mmgA mmgA spo0A spo0A dnaJ dnaJ phoP phoP pgi pgi copZ copZ lutC lutC lutB lutB ppaX ppaX hpf hpf hag hag flgL flgL alsD alsD acdA acdA narJ narJ narH narH narG narG qoxA qoxA cydA cydA hutP hutP yhfS yhfS acoL acoL ydeN ydeN pdhD pdhD hfq hfq spoIIAB spoIIAB lpdV lpdV buk buk
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
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ptbPhosphate butyryl coenzyme A transferase; Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate; Belongs to the phosphate acetyltransferase and butyryltransferase family. (299 aa)
mmgB3-hydroxybutyryl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (287 aa)
gabDSuccinate-semialdehyde dehydrogenase; Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate. (462 aa)
abhTranscriptional regulator; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator; To B.subtilis AbrB and SpoVT. (92 aa)
gabT4-aminobutyrate aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (436 aa)
nasDAssimilatory nitrite reductase subunit; Required for nitrite assimilation. (805 aa)
nasEAssimilatory nitrite reductase subunit; Required for nitrite assimilation. Required for activity of the reductase (By similarity). (106 aa)
spoIIESpoIIAA-phosphate serine phosphatase; Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation. (827 aa)
mmgADegradative acetoacetyl-CoA thiolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
spo0AResponse regulator; May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box). (267 aa)
dnaJCo-factor of molecular chaperone; 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 betwe [...] (375 aa)
phoPTwo-component response regulator; Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase. (240 aa)
pgiGlucose-6-phosphate isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the GPI family. (450 aa)
copZCopper insertion chaperone and transporter component; Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA. Functions in E.coli to transfer Cu(+) to CopA missing its first metal-binding domain. (69 aa)
lutCComponent of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present. (240 aa)
lutBComponent of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present. (479 aa)
ppaXP-Ser-HPr phosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool; Belongs to the HAD-like hydrolase superfamily. PpaX family. (216 aa)
hpfRibosome-associated sigma 54 modulation protein; Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth. May not be the only factor implicated. Might negatively regulate the activity of the sigma-54 factor (SigL). (189 aa)
hagFlagellin protein; Flagellin is the subunit which polymerizes to form the filaments of bacterial flagella. Assembly into flagella requires FliW. Acts as a homeostatic autoinhibitory regulator to control its own cytoplasmic levels. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagell [...] (304 aa)
flgLFlagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. (298 aa)
alsDAlpha-acetolactate decarboxylase; Converts acetolactate into acetoin, which can be excreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage; Belongs to the alpha-acetolactate decarboxylase family. (255 aa)
acdAacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids. (379 aa)
narJNitrate reductase molybdenum cofactor assembly chaperone NarJ; Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase. Belongs to the NarJ/NarW family. (184 aa)
narHNitrate reductase (beta subunit); The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. (487 aa)
narGNitrate reductase (alpha subunit); The alpha chain is the actual site of nitrate reduction. (1228 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)
cydACytochrome bb' ubiquinol oxidase (subunit I); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (468 aa)
hutPTranscriptional antiterminator; Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization; Belongs to the HutP family. (148 aa)
yhfSPutative acetyl-CoA C-acetyltransferase; May be involved in fatty acid metabolism; Belongs to the thiolase-like superfamily. Thiolase family. (364 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)
ydeNAlpha/beta hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the RBBP9 family. (190 aa)
pdhDDihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa)
hfqHfq RNA chaperone; 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. Belongs to the Hfq family. (73 aa)
spoIIABAnti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. (146 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)
bukBranched-chain fatty-acid kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the acetokinase family. (363 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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