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
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[Homology]
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grpEHsp 24 DnaK nucleotide exchange factor; 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 [...] (203 aa)    
Predicted Functional Partners:
hrcA
Conserved protein of unknown function; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.994
groL
60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.991
dnaK
Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.991
dnaJ
Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...]
 
 
 0.979
groS
10 kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.977
hscA
Chaperone protein HscA homolog; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
 
 0.957
PSHAa2176
Putative heat shock protein (Hsp70 family), actin-like ATPase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy.
  
 0.933
clpB
ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; 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.
  
 
 0.904
cbpA
Curved DNA-binding protein, co-chaperone of DnaK (Hsp40 family); Function of strongly homologous gene; molecular chaperone.
 
 
 0.903
hslU
ATPase component of the HslUV protease, also functions as molecular chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
  
 0.880
Your Current Organism:
Pseudoalteromonas haloplanktis
NCBI taxonomy Id: 326442
Other names: P. haloplanktis TAC125, Pseudoalteromonas haloplanktis TAC125, Pseudoalteromonas haloplanktis str. TAC125, Pseudoalteromonas haloplanktis strain TAC125
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