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
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[Homology]
Score
grpECo-chaperone 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-depend [...] (248 aa)    
Predicted Functional Partners:
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.995
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.992
dnaK-3
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.992
EKF04570.1
Putative heat shock protein 70 DnaK; KEGG: ava:Ava_0434 2.4e-54 serine/threonine protein kinase K00908; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family.
 
 0.980
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 [...]
 
 
 0.979
EKF00763.1
Putative heat shock protein 70 DnaK; KEGG: chl:Chy400_2236 1.1e-110 chaperone protein DnaK K04043; Psort location: Cytoplasmic, score: 9.97; Belongs to the heat shock protein 70 family.
 
 0.979
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.976
EKF04740.1
Heat shock protein 70 DnaK; KEGG: pmo:Pmob_1649 1.9e-20 dnaK; molecular chaperone DnaK K04043; Belongs to the heat shock protein 70 family.
 
 0.975
groL-2
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.966
groL-3
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.966
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.