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
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
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 [...]
 
 0.944
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 [...]
 
 0.944
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.939
Dred_3115
PFAM: Heat shock protein 70; KEGG: tma:TM0373 dnaK protein.
 
 0.933
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 
 0.903
Dred_3116
Hypothetical protein.
  
 0.871
Dred_1087
CheC, inhibitor of MCP methylation; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein; KEGG: chy:CHY_1020 flagellar motor switch protein.
    
 
 0.870
Dred_2380
CheC, inhibitor of MCP methylation; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein; KEGG: chy:CHY_1020 flagellar motor switch protein.
    
 
 0.870
Dred_0971
Plasmid segregation actin-type ATPase ParM; KEGG: mta:Moth_0345 hypothetical protein.
  
 0.842
Your Current Organism:
Desulfotomaculum reducens
NCBI taxonomy Id: 349161
Other names: D. reducens MI-1, Desulfotomaculum reducens MI-1, Desulfotomaculum reducens str. MI-1, Desulfotomaculum reducens strain MI-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.