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
dnaKChaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (643 aa)    
Predicted Functional Partners:
dnaJ
DnaJ molecular chaperone; 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, [...]
 0.999
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 [...]
 
 0.998
ED21_19732
COG2214 DnaJ-class molecular chaperone.
 0.997
groEL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.995
ED21_19617
ATPase; COG0542 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
 
 
 0.989
clpB
ATP-dependent Clp protease; 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.
  
 
 0.988
ED21_21384
COG2214 DnaJ-class molecular chaperone.
  
 0.983
ED21_24631
DnaJ-class molecular chaperone; COG0183 Acetyl-CoA acetyltransferase.
  
 0.983
ED21_19987
Hypothetical protein; COG2214 DnaJ-class molecular chaperone.
  
 0.981
ED21_25582
Hypothetical protein; COG0790 FOG: TPR repeat, SEL1 subfamily.
   
 0.979
Your Current Organism:
Erythrobacter sp. SD21
NCBI taxonomy Id: 161528
Other names: E. sp. SD-21, Erythrobacter sp. SD-21
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