STRINGSTRING
clpB clpB dnaK dnaK clpP clpP grpE grpE ACS38130.1 ACS38130.1 dnaJ dnaJ ibpA-3 ibpA-3 ibpA-2 ibpA-2 ibpA ibpA hslU hslU htpG htpG
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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
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; Belongs to the ClpA/ClpB family. (874 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.984
clpP
ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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.
  
 
 0.964
grpE
Putative heat shock protein (HSP-70 COFACTOR), 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 c [...]
  
 
 0.955
ACS38130.1
Molecular chaperone, HSP70 class; Function of strongly homologous gene; factor.
  
 
 0.945
dnaJ
Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...]
  
 
 0.943
ibpA-3
Heat shock chaperone; Function of homologous gene experimentally demonstrated in an other organism; factor; Belongs to the small heat shock protein (HSP20) family.
  
 
 0.928
ibpA-2
Small heat shock protein; Function of strongly homologous gene; factor; Belongs to the small heat shock protein (HSP20) family.
  
 
 0.917
ibpA
Small heat shock protein; Function of strongly homologous gene; factor; Belongs to the small heat shock protein (HSP20) family.
  
 
 0.910
hslU
ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.899
htpG
Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity.
  
 
 0.850
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.