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sodF sodF sigF sigF lpdV lpdV sodA sodA hag hag vpr vpr epr epr srfAC srfAC sigW sigW mpr mpr amyE amyE acoL acoL aprE aprE malA malA wprA wprA nprB nprB pdhD pdhD nprE nprE bpr bpr
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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
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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:
sodFSuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. (281 aa)
sigFRNA polymerase sporulation-specific sigma factor (sigma-F); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes. Interaction with SpoIIAB inhibits sigma-F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore. Responsible for expression of csfB (the anti-sigma-G factor Gin). (255 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)
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)
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)
vprExtracellular serine protease; Not required for growth or sporulation. (806 aa)
eprExtracellular serine protease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S8 family. (645 aa)
srfACSurfactin synthetase; Probably activates a leucine. (1275 aa)
sigWRNA polymerase ECF(extracytoplasmic function)-type sigma factor W; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides , alkaline pH , transport processes and detoxification. (187 aa)
mprExtracellular glutamyl-endopeptidase; Evidence 1c: Function experimentally demonstrated in the studied genus; Product type e: enzyme; Belongs to the peptidase S1B family. (313 aa)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 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)
aprESerine alkaline protease (subtilisin E); Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides; Belongs to the peptidase S8 family. (381 aa)
malA6-phospho-alpha-glucosidase; Hydrolyzes maltose-6'-phosphate and trehalose-6'-phosphate. Is involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP- PTS). Is also able to significantly catalyze the hydrolysis of both 6- phospho-alpha- and 6-phospho-beta-glucosides containing activated leaving groups such as p-nitrophenol and does so with retention and inversion, respectively, of the substrate anomeric configuration. (449 aa)
wprACell wall-associated protease; CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges; Belongs to the peptidase S8 family. (894 aa)
nprBExtracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. (538 aa)
pdhDDihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa)
nprEExtracellular neutral metalloprotease; Extracellular zinc metalloprotease; Belongs to the peptidase M4 family. (521 aa)
bprEvidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (1433 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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