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
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[Homology]
Score
grpEProtein 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-dependent i [...] (245 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.995
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 [...]
 
 
 0.989
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.972
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.932
AEJ60430.1
Peptidoglycan-binding lysin domain-containing protein; PFAM: LysM domain; InterPro IPR018392:IPR002482; KEGG: sta:STHERM_c01550 hypothetical protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup; SPTR: Peptidoglycan-binding lysin domain.
  
 
 0.921
AEJ62118.1
KEGG: sta:STHERM_c17890 hypothetical protein; SPTR: Putative uncharacterized protein.
  
 
 0.921
AEJ61281.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: sta:STHERM_c09840 molecular chaperone protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
 
 
 0.916
hslU
ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
  
 0.893
hslV
ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.871
AEJ60847.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; InterPro IPR001623; KEGG: sta:STHERM_c05450 hypothetical protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
  
 
 0.852
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.