STRINGSTRING
Atu0988 Atu0988 grpE grpE groEL groEL dnaJ-4 dnaJ-4 dnaJ dnaJ dnaJ-2 dnaJ-2 dnaJ-3 dnaJ-3 clpA clpA clpB clpB clpB-2 clpB-2 groES groES
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
Atu0988Molecular chaperone, Hsp70 family. (432 aa)    
Predicted Functional Partners:
grpE
GRPE 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-dependent i [...]
  
 0.944
groEL
GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.908
dnaJ-4
Molecular chaperone, DnaJ family.
 
 0.902
dnaJ
Molecular chaperone, DnaJ family; 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 betwe [...]
  
 0.899
dnaJ-2
Molecular chaperone, DnaJ family.
  
 0.899
dnaJ-3
Molecular chaperone, DnaJ family.
  
 0.892
clpA
ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.866
clpB
ATP-dependent Clp protease, ATP-binding subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the [...]
  
 
 0.866
clpB-2
ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.866
groES
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.855
Your Current Organism:
Agrobacterium fabrum
NCBI taxonomy Id: 176299
Other names: A. fabrum str. C58, Agrobacterium fabrum str. C58, Agrobacterium tumefaciens (strain C58 / ATCC 33970), Agrobacterium tumefaciens (strain C58), Agrobacterium tumefaciens str. C58, Agrobacterium tumefaciens str. C58 (Cereon), Agrobacterium tumefaciens str. C58 (Dupont), Agrobacterium tumefaciens str. C58 (U. Washington), Rhizobium radiobacter str. C58 (Cereon), Rhizobium radiobacter str. C58 (Dupont), Rhizobium radiobacter str. C58 (U. Washington)
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.