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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
groL1Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa)    
Predicted Functional Partners:
groS1
Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.998
groS2
Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.996
grpE
Heat shock protein GrpE; 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- [...]
 
 0.975
dnaJ
dnaJ protein; 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, DnaK and Gr [...]
 
 0.975
htpG
Heat shock protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family.
   
 
 0.966
dnaK
dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.941
groL2
Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
0.901
VC_1386
Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; identified by sequence similarity; putative.
  
 0.881
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
   
 0.880
VC_0977
Conserved hypothetical protein; Identified by Glimmer2; putative.
   
 
 0.879
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.