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
dnaJ-2Chaperone 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 [...] (381 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK (heat shock protein 70); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.983
grpE
Protein 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 roun [...]
 
 
 0.974
htpG
Chaperone protein HtpG (heat shock protein HtpG); Molecular chaperone. Has ATPase activity.
  
 0.971
hscA
Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
 0.948
groL1
60 kda chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.902
hslU
ATP-dependent hsl protease ATP-binding subunit HslU (heat shock protein HslU); 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.
  
 
 0.898
CED71679.1
Putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family.
  
 0.890
CED71680.1
Putative heat-shock chaperone protein.
  
 0.890
hslV
ATP-dependent protease HslV (heat shock protein HslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.862
CED71586.1
Putative heat shock protein.
  
 0.861
Your Current Organism:
Aliivibrio wodanis
NCBI taxonomy Id: 80852
Other names: A. wodanis, ATCC BAA-104, Aliivibrio wodanis (Lunder et al. 2000) Urbanczyk et al. 2007, DSM 22225, LMG 24053, LMG:24053, NCIMB 13582, Vibrio wodanis, Vibrio wodanis Lunder et al. 2000, strain NVI 88/441
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.