STRINGSTRING
dnaK dnaK dnaJ dnaJ htpG htpG grpE grpE groL groL clpB clpB ETA_09880 ETA_09880 ETA_06350 ETA_06350 groS groS clpA clpA djlA djlA
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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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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dnaKChaperone protein dnaK (Heat shock 70 kDa protein); Acts as a chaperone; Belongs to the heat shock protein 70 family. (637 aa)    
Predicted Functional Partners:
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 [...]
 0.999
htpG
Heat shock protein (High temperature protein G); Molecular chaperone. Has ATPase activity.
   
 0.983
grpE
Heat shock 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-depen [...]
 
 0.980
groL
60 kDa chaperonin (Protein Cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.970
clpB
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.
 
 
 0.933
ETA_09880
Lambdoid prophage Qin antitermination protein Q-like protein; silverDB:etchr00979.
  
 0.904
ETA_06350
Putative ClpA/B-type chaperone; silverDB:etchr00627; Belongs to the ClpA/ClpB family.
  
 
 0.898
groS
10 kDa chaperonin (Protein Cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.887
clpA
ATP-dependent Clp protease ATP-binding subunit; silverDB:etchr02149; Belongs to the ClpA/ClpB family.
 
 
 0.878
djlA
DnaJ like chaperone protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
  
 
 0.822
Your Current Organism:
Erwinia tasmaniensis
NCBI taxonomy Id: 465817
Other names: E. tasmaniensis Et1/99, Erwinia tasmaniensis Et1/99, Erwinia tasmaniensis str. Et1/99, Erwinia tasmaniensis strain Et1/99
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