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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] (197 aa)    
Predicted Functional Partners:
clpC
Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.
 
 
 0.999
clpE
ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress.
 
 
 0.999
clpX
Protein unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Probably the major protease that degrades proteins tagged by trans-translation.
 
 0.999
mecA
Adaptor protein controlling oligomerization of the AAA+ protein ClpC; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
   
  
 0.984
clpY
Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily.
 
  
 0.984
dnaK
Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 
 0.982
hrcA
Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
   
  
 0.973
groEL
Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.972
clpQ
Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily.
  
 
 0.970
mcsB
Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...]
   
  
 0.968
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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