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
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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yfkMGeneral stress protein 18; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins. (172 aa)    
Predicted Functional Partners:
rsbW
Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
   
  
 0.978
rsbV
Anti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B.
   
  
 0.963
ysnF
Putative stress response protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; phenotype.
  
  
 0.947
yflT
Heat stress induced protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor.
   
  
 0.928
yhdN
Aldo/keto reductase specific for NADPH; Aldo-keto reductase (AKR) that displays broad substrate specificity in vitro. Is able to reduce the standard AKR substrates DL- glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde, benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use NADH as a cosubstrate. Does not act on glucose, 2-pyridine carboxyaldehyde, fructose and xylose. The physiological function of this enzyme is not clear. May play a role in bacterial stress response and/or in detoxification of reactive aldehydes. Belongs to the aldo/keto reductase family. A [...]
  
  
 0.895
ydaE
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 10220166; Belongs to the D-lyxose ketol-isomerase family.
   
  
 0.875
ydaG
Putative general stress protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor.
  
  
 0.825
gspA
Putative glycosyl transferase (general stress protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
   
  
 0.812
ybyB
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
   
  
 0.779
ywzA
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
  
 0.771
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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