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:
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
grpEGrpE 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 [...] (206 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.974
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 [...]
 
 
 0.953
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.951
Bmur_0008
KEGG: bhy:BHWA1_00223 putative chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein.
 
 
 0.943
Bmur_0988
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
  
  
 0.869
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.856
Bmur_2180
KEGG: bhy:BHWA1_02524 hypothetical protein.
  
 
 0.842
Bmur_0861
ATPase AAA-2 domain protein; KEGG: bhy:BHWA1_01228 hemolysin B; ClpA, ATPases with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; UvrB/UvrC protein; Clp domain protein; Clp ATPase-like; AAA ATPase central domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
  
 
 0.828
clpB
ATP-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.
  
 
 0.828
Your Current Organism:
Brachyspira murdochii
NCBI taxonomy Id: 526224
Other names: B. murdochii DSM 12563, Brachyspira murdochii 56-150, Brachyspira murdochii ATCC 51284, Brachyspira murdochii CIP 105832, Brachyspira murdochii DSM 12563, Brachyspira murdochii str. DSM 12563, Brachyspira murdochii strain DSM 12563
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.