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clpB protein (Gallibacterium anatis) - STRING interaction network
"clpB" - Protein disaggregation chaperone in Gallibacterium anatis
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Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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clpBProtein disaggregation chaperone; 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 (857 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone (639 aa)
   
 
  0.980
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 [...] (373 aa)
   
  0.978
grpE
Heat shock protein 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- [...] (196 aa)
   
 
  0.973
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 (195 aa)
   
 
  0.948
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (628 aa)
   
 
  0.935
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (553 aa)
   
 
  0.867
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
   
 
  0.856
hscA
Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (617 aa)
   
 
  0.826
zwf
Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone (499 aa)
     
 
  0.813
clpX
ATP-dependent protease ATP-binding subunit ClpX; 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)
   
 
  0.813
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
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