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clpB1 protein (Synechococcus elongatus PCC7942) - STRING interaction network
"clpB1" - Chaperone protein ClpB 1 in Synechococcus elongatus PCC7942
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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Cooccurence
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[Homology]
Score
clpB1Chaperone protein ClpB 1; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary for thermotolerance; Belongs [...] (883 aa)    
Predicted Functional Partners:
dnaK2
Chaperone protein dnaK2; Acts as a chaperone (634 aa)
 
 
  0.786
dnaK3
Chaperone protein dnaK3; Acts as a chaperone (749 aa)
 
 
  0.784
clpR
Putative ATP-dependent Clp protease proteolytic subunit-like; Has lost the two conserved residues (Ser and His) proposed to be part of the active site. Therefore it could be inactive (228 aa)
     
 
  0.781
clpP3
ATP-dependent Clp protease proteolytic subunit 3; 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; Belongs to the peptidase S14 family (199 aa)
     
 
  0.781
SEM0037
annotation not available (638 aa)
   
 
  0.780
ABB56717.1
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (555 aa)
 
 
  0.757
dnaK1
Chaperone protein dnaK1; Acts as a chaperone (655 aa)
   
 
  0.755
ABB57819.1
annotation not available (326 aa)
 
 
  0.744
mopA
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
   
 
  0.735
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (103 aa)
   
 
  0.719
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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