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
dnaK1Chaperone, DnaK-like protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (632 aa)    
Predicted Functional Partners:
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 [...]
 
 0.990
dnaJ
Chaperone Hsp40/DnaJ, 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. Several rounds of ATP-dependent intera [...]
 0.987
groL
Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.948
htpG
Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity.
   
 0.948
VF_1108
Chaperone protein DnaJ-like protein.
 0.936
groS
Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.910
dnaK
Chaperone Hsp70/DnaK, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 
0.900
VF_1477
Tetratricopeptide repeat family protein.
  
 0.886
clpB
Protein disaggregation chaperone; 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.
  
 
 0.884
clpA
ATPase and specificity subunit of ClpA-ClpP ATP-dependent serine protease, chaperone activity; Belongs to the ClpA/ClpB family.
  
 
 0.858
Your Current Organism:
Aliivibrio fischeri
NCBI taxonomy Id: 312309
Other names: A. fischeri ES114, Aliivibrio fischeri ES114, Vibrio fischeri ES114, Vibrio fischeri str. ES114, Vibrio fischeri strain ES114
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.