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
dnaKDnaK: chaperone Hsp70 family; Acts as a chaperone; Belongs to the heat shock protein 70 family. (636 aa)    
Predicted Functional Partners:
grpE
GrpE: HSP70 cofactor; 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-dep [...]
 
 0.995
dnaJ
DnaJ: chaperone 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, [...]
 0.992
htpG
HtpG: chaperone protein; Molecular chaperone. Has ATPase activity.
  
 0.982
CCK81905.1
Heat shock protein, DnaJ domain.
 0.955
groL
GroL: 60kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.945
CCK82055.1
Heat shock protein, DnaJ domain.
 
 0.931
CCK78602.1
Putative heat shock protein related to DnaJ.
 
 0.930
groS
GroS: 10kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.900
clpB
ClpB: 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.
  
 
 0.845
clpA
ClpA: ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.845
Your Current Organism:
Desulfobacula toluolica
NCBI taxonomy Id: 651182
Other names: D. toluolica Tol2, Desulfobacula toluolica DSM 7467, Desulfobacula toluolica Tol2, Desulfobacula toluolica str. Tol2, Desulfobacula toluolica strain Tol2
Server load: medium (42%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.