STRINGSTRING
amyE amyE sipU sipU ltaSA ltaSA ltaSB ltaSB rbn rbn prsA prsA sipV sipV wprA wprA htrA htrA sipT sipT nprE nprE rseP rseP prsW prsW sipS sipS sipW sipW ltaSC ltaSC yqeZ yqeZ dnaK dnaK secDF secDF trxA trxA sppA sppA htrB htrB cssR cssR cssS cssS ltaSP ltaSP secG secG upp upp
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.
Node Color
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:
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 aa)
sipUType I signal peptidase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S26 family. (187 aa)
ltaSAExported glycerol phosphate lipoteichoic acid synthetase and anion-binding protein; Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate. (639 aa)
ltaSBEnzyme responsible for polyglycerolphosphate LTA synthesis; Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate; Belongs to the LTA synthase family. (649 aa)
rbnPutative ribonuclease BN; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (275 aa)
prsAMolecular chaperone lipoprotein; Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo; Belongs to the PrsA family. (292 aa)
sipVType I signal peptidase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S26 family. (168 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)
htrAMembrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (449 aa)
sipTType I signal peptidase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S26 family. (193 aa)
nprEExtracellular neutral metalloprotease; Extracellular zinc metalloprotease; Belongs to the peptidase M4 family. (521 aa)
rsePRegulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. (422 aa)
prsWProtease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...] (218 aa)
sipSType I signal peptidase; Not essential for cell viability, but required for efficient secretion of many proteins. (184 aa)
sipWType I signal peptidase; Required for the cleavage of the signal sequence of TasA and TapA, which are involved in biofilm formation. Belongs to the peptidase S26B family. (190 aa)
ltaSCEnzyme responsible for polyglycerolphosphate LTA synthesis; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the LTA synthase family. (638 aa)
yqeZPutative membrane bound hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (437 aa)
dnaKMolecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (611 aa)
secDFProtein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily. (737 aa)
trxAThioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. (104 aa)
sppASignal peptide peptidase; Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides. Belongs to the peptidase S49 family. (335 aa)
htrBHtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (458 aa)
cssRTwo-component response regulator; Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. (225 aa)
cssSTwo-component sensor histidine kinase; Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation. (451 aa)
ltaSPPrimase of polyglycerolphosphate lipoteichoic acid (LTA) synthesis; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the LTA synthase family. (617 aa)
secGPreprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity). (76 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (209 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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.