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
EJT06878.1Molecular chaperone heat shock protein (HSP70); COG0443 Molecular chaperone. (430 aa)    
Predicted Functional Partners:
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- [...]
  
 0.996
EJT03420.1
Curved DNA-binding protein; COG2214 DnaJ-class molecular chaperone.
 
 0.992
EJT06474.1
Heat shock protein DnaJ domain protein; COG2214 DnaJ-class molecular chaperone.
 
 0.990
dnaJ
Chaperone 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 [...]
 
 0.990
EJT06469.1
DnaJ family molecular chaperone.
  
 0.988
EJT03644.1
Heat shock protein DnaJ domain-containing protein; COG2214 DnaJ-class molecular chaperone.
  
 0.988
EJT05114.1
COG1076 DnaJ-domain-containing proteins 1.
  
 0.985
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 0.981
groEL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.981
EJT05758.1
ATP-dependent Clp protease ATP-binding subunit clpA; COG0542 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.980
Your Current Organism:
Rhizobium sp. CCGE510
NCBI taxonomy Id: 1132836
Other names: R. sp. CCGE 510, Rhizobium sp. CCGE 510
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