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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
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; Belongs to the ClpA/ClpB family. (866 aa)    
Predicted Functional Partners:
dnaJ
Chaperone DnaJ domain protein; 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 [...]
 
 
 0.973
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.972
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.926
AEG58969.1
KEGG: adg:Adeg_0813 hypothetical protein.
  
 
 0.890
AEG61951.1
KEGG: tmt:Tmath_0071 StbA family protein.
  
 
 0.890
clpP
ATP-dependent Clp protease, proteolytic subunit ClpP; 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.
   
 
 0.863
AEG61753.1
PFAM: peptidase S14 ClpP; KEGG: cce:Ccel_2835 peptidase S14 ClpP; Belongs to the peptidase S14 family.
   
 
 0.863
clpP-2
ATP-dependent Clp protease, proteolytic subunit ClpP; 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.
   
 
 0.863
AEG60181.1
PFAM: peptidase S14 ClpP; KEGG: drm:Dred_1937 peptidase S14, ClpP; Belongs to the peptidase S14 family.
   
 
 0.861
grpE
GrpE protein; 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-dependent i [...]
  
 
 0.856
Your Current Organism:
Desulfotomaculum ruminis
NCBI taxonomy Id: 696281
Other names: D. ruminis DSM 2154, Desulfotomaculum ruminis ATCC 23193, Desulfotomaculum ruminis DL, Desulfotomaculum ruminis DSM 2154, Desulfotomaculum ruminis str. DSM 2154, Desulfotomaculum ruminis strain DSM 2154
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.