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.
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
dnaKChaperone protein DnaK; Acts as a chaperone. (644 aa)    
Predicted Functional Partners:
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 [...]
 0.999
grpE
Molecular chaperone 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. [...]
 
 0.999
AGB32165.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 0.993
AGB31890.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 0.986
AGB30123.1
Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.972
AGB30354.1
Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.971
AGB32996.1
PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.959
AGB33509.1
PFAM: Tetratricopeptide repeat.
 
 0.943
rpl32e
PFAM: Ribosomal protein L32; Belongs to the eukaryotic ribosomal protein eL32 family.
   
 
 0.936
AGB33520.1
PFAM: NifU-like N terminal domain; TIGRFAM: SUF system FeS assembly protein, NifU family.
  
 0.936
Your Current Organism:
Natrinema pellirubrum
NCBI taxonomy Id: 797303
Other names: N. pellirubrum DSM 15624, Natrinema pellirubrum DSM 15624, Natrinema pellirubrum JCM 10476, Natrinema pellirubrum NCIMB 786, Natrinema pellirubrum str. DSM 15624, Natrinema pellirubrum strain DSM 15624
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.