STRINGSTRING
dnaK dnaK dnaJ dnaJ htpG htpG grpE grpE groL groL Ppha_1809 Ppha_1809 Ppha_0992 Ppha_0992 Ppha_0245 Ppha_0245 Ppha_2617 Ppha_2617 Ppha_2812 Ppha_2812 Ppha_0366 Ppha_0366
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
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (640 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 [...]
 0.990
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.964
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 [...]
 
 0.963
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.893
Ppha_1809
PFAM: heat shock protein DnaJ domain protein; Gas vesicle synthesis GvpLGvpF; KEGG: plt:Plut_0698 hypothetical protein.
  
 0.860
Ppha_0992
KEGG: cch:Cag_1146 hypothetical protein.
  
 0.840
Ppha_0245
PFAM: AAA ATPase central domain protein; Clp domain protein; SMART: AAA ATPase; KEGG: cph:Cpha266_2449 AAA ATPase, central domain protein; Belongs to the ClpA/ClpB family.
  
 
 0.787
Ppha_2617
PFAM: UvrB/UvrC protein; AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; KEGG: cph:Cpha266_0334 ATPase AAA-2 domain protein; Belongs to the ClpA/ClpB family.
  
 
 0.787
Ppha_2812
ATPase AAA-2 domain protein; PFAM: ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; SMART: AAA ATPase; KEGG: cph:Cpha266_2577 ATPase AAA-2 domain protein.
  
 
 0.787
Ppha_0366
PFAM: nitrogen-fixing NifU domain protein; BFD domain protein [2Fe-2S]-binding domain protein; KEGG: cph:Cpha266_2362 nitrogen-fixing NifU domain protein.
 
 
 0.778
Your Current Organism:
Pelodictyon phaeoclathratiforme
NCBI taxonomy Id: 324925
Other names: P. phaeoclathratiforme BU-1, Pelodictyon phaeoclathratiforme BU-1, Pelodictyon phaeoclathratiforme DSM 5477, Pelodictyon phaeoclathratiforme str. BU-1, Pelodictyon phaeoclathratiforme strain BU-1
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.