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
dnaJChaperone 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 [...] (378 aa)    
Predicted Functional Partners:
AFZ46264.1
AMP-dependent synthetase and ligase; PFAM: AMP-binding enzyme; COGs: COG0318 Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; InterPro IPR020845:IPR000873; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: AMP-dependent synthetase and ligase; SPTR: Beta-ketoacyl synthase.
  
 
 0.990
AFZ46265.1
Beta-ketoacyl synthase; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Beta-ketoacyl synthase, N-terminal domain; AMP-binding enzyme; Sulfotransferase domain; Beta-ketoacyl synthase, C-terminal domain; COGs: COG3321 Polyketide synthase modules and related protein; InterProIPR000639:IPR009081:IPR006162:IPR018201:IPR 000873:IPR006163:IPR014030:IPR014031:IPR014043:IPR013968:I PR000863:IPR000073; KEGG: cyc:PCC7424_1874 beta-ketoacyl synthase; PFAM: Beta-ketoacyl synthase; phosphopantetheine-binding; AMP-dependent synthetase and ligase; Acyl transferase; KR do [...]
  
 
 0.990
dnaK-3
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.974
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.972
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.946
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 [...]
 
 
 0.935
AFZ46781.1
PFAM: Hsp70 protein; COGs: COG0443 Molecular chaperone; InterPro IPR018181:IPR013126:IPR001023; KEGG: cyc:PCC7424_0171 heat shock protein 70; PFAM: Heat shock protein 70; SPTR: Heat shock protein 70.
  
 0.899
AFZ47450.1
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity.
  
 0.752
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.700
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.696
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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