STRINGSTRING
STRING protein interaction network
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
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)    
Predicted Functional Partners:
cssR
Two-component response regulator; Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress.
  
  
 0.980
cssS
Two-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.
  
  
 0.975
htrA
Membrane 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.
  
 
0.974
wprA
Cell wall-associated protease; CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges; Belongs to the peptidase S8 family.
   
  
 0.796
prsA
Molecular 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.
  
  
 0.793
nprE
Extracellular neutral metalloprotease; Extracellular zinc metalloprotease; Belongs to the peptidase M4 family.
      
 0.749
rseP
Regulator 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.
 
  
 0.735
aprE
Serine 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.
   
  
 0.727
bpr
Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
   
  
 0.726
epr
Extracellular serine protease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S8 family.
   
  
 0.724
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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