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
RPE_0414KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. (417 aa)    
Predicted Functional Partners:
RPE_2484
PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like.
  
 0.990
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 0.990
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 [...]
  
 0.987
dnaJ
Chaperone protein 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, D [...]
 
 0.967
RPE_4592
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: rpc:RPC_1138 chaperone DnaJ-like.
  
 0.962
RPE_0137
PFAM: heat shock protein DnaJ domain protein; KEGG: rpc:RPC_0536 heat shock protein DnaJ-like.
  
 0.958
RPE_3408
PFAM: heat shock protein DnaJ domain protein; KEGG: rpc:RPC_3329 heat shock protein DnaJ-like.
  
 0.955
RPE_2641
PFAM: ATPase AAA-2 domain protein; SMART: AAA ATPase; KEGG: gox:GOX1577 ATP-dependent Clp protease ATP-binding subunit ClpA.
  
 
 0.953
RPE_3404
KEGG: rpb:RPB_2396 AAA_5 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase, central domain protein; Clp N terminal domain protein; ATPase associated with various cellular activities, AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
  
 
 0.953
clpB
ATPase AAA-2 domain protein; 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.
  
 
 0.953
Your Current Organism:
Rhodopseudomonas palustris BisA53
NCBI taxonomy Id: 316055
Other names: R. palustris BisA53, Rhodopseudomonas palustris str. BisA53, Rhodopseudomonas palustris strain BisA53
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.