STRINGSTRING
dnaK dnaK dnaJ dnaJ grpE grpE RPC_1138 RPC_1138 htpG htpG RPC_4138 RPC_4138 RPC_3324 RPC_3324 clpB clpB RPC_0536 RPC_0536 RPC_3329 RPC_3329 groL2 groL2
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:
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[Homology]
Score
dnaKChaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (632 aa)    
Predicted Functional Partners:
dnaJ
Chaperone 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, DnaK and [...]
 0.999
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 [...]
 
 0.993
RPC_1138
Chaperone DnaJ-like.
 0.993
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
 
 0.990
RPC_4138
ATP-binding region, ATPase-like.
 
 0.989
RPC_3324
ATP-dependent Clp protease ATP-binding subunit ClpA; Belongs to the ClpA/ClpB family.
 
 
 0.975
clpB
ATPase AAA-2; 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.
 
 
 0.974
RPC_0536
Heat shock protein DnaJ-like.
  
 0.972
RPC_3329
Heat shock protein DnaJ-like.
  
 0.968
groL2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.955
Your Current Organism:
Rhodopseudomonas palustris BisB18
NCBI taxonomy Id: 316056
Other names: R. palustris BisB18, Rhodopseudomonas palustris str. BisB18, Rhodopseudomonas palustris strain BisB18
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