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
grpEGrpE 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 [...] (180 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone.
 
 
 0.987
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 [...]
 
 
 0.970
dnaK-2
Chaperone protein DnaK; Acts as a chaperone.
 
 
 0.964
dnaJ-2
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 [...]
 
 
 0.950
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.886
Mboo_1090
PFAM: chaperonin Cpn10; KEGG: mac:MA0630 groES protein (Cpn10); Belongs to the GroES chaperonin family.
  
 
 0.877
Mboo_0199
TIGRFAM: thermosome; PFAM: chaperonin Cpn60/TCP-1; KEGG: mhu:Mhun_2549 thermosome.
 
 0.868
Mboo_0315
TIGRFAM: thermosome; PFAM: chaperonin Cpn60/TCP-1; KEGG: mhu:Mhun_2549 thermosome.
 
 0.867
Mboo_0320
PFAM: chaperonin Cpn60/TCP-1; KEGG: mhu:Mhun_0972 chaperonin Cpn60/TCP-1; Belongs to the TCP-1 chaperonin family.
 
 0.865
Mboo_2395
PFAM: chaperonin Cpn60/TCP-1; KEGG: mhu:Mhun_0972 chaperonin Cpn60/TCP-1; Belongs to the TCP-1 chaperonin family.
 
 0.863
Your Current Organism:
Methanoregula boonei
NCBI taxonomy Id: 456442
Other names: Candidatus Methanoregula boonei 6A8, M. boonei 6A8, Methanoregula boonei 6A8, Methanoregula boonei str. 6A8, Methanoregula boonei strain 6A8, methanogenic archaeon 6A8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.