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clpB protein (Midichloria mitochondrii) - STRING interaction network
"clpB" - ATP-dependent chaperone ClpB in Midichloria mitochondrii
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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clpBATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE (862 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone (631 aa)
   
 
  0.997
clpP
ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (216 aa)
   
 
  0.994
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (385 aa)
   
  0.987
grpE
Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...] (183 aa)
   
 
  0.967
hscA
Chaperone protein, HscA (499 aa)
   
 
  0.922
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity (579 aa)
   
 
  0.904
ftsH
Cell division protease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (644 aa)
   
 
  0.902
clpX
ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (415 aa)
   
 
  0.889
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (385 aa)
   
 
  0.868
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
   
 
  0.833
Your Current Organism:
Midichloria mitochondrii
NCBI taxonomy Id: 696127
Other names: C. Midichloria, C. Midichloria mitochondrii, C. Midichloria mitochondrii IricVA, Candidatus Midichloria, Candidatus Midichloria mitochondrii, Candidatus Midichloria mitochondrii IricVA, Candidatus Midichloria mitochondrii str. IricVA, Candidatus Midichloria mitochondrii strain IricVA, Ixodes ricinus endosymbiont, Ixodes ricinus endosymbiont 1 (IricES1), Midichloria, Midichloria mitochondrii, Midichloria mitochondrii IricVA, endosymbiont of Ixodes ricinus
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