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:
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[Homology]
Score
grpEGrpE 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 [...] (203 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.991
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.965
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 [...]
 
 
 0.960
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.917
ADR23420.1
Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623: IPR003095; KEGG: ddi:DDB_G0288639 DNAJ heat shock N-terminal domain-containing protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ homolog subfamily C member 7 homolog; PFAM: DnaJ domain.
 
 
 0.882
ADR22763.1
Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623: IPR013026: IPR003095; KEGG: chu:CHU_1443 DnaJ class chaperone; heat shock protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DNAJ class chaperone; heat shock protein; PFAM: DnaJ domain.
 
 
 0.871
hslU
Heat shock protein HslVU, ATPase 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.
  
  
 0.805
hslV
ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.785
ADR21698.1
ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR001270: IPR004176: IPR003959: IPR001943: IPR 013093: IPR019489: IPR003593: IPR018368; KEGG: chu:CHU_1079 ATP-dependent Clp protease, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPase; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); [...]
 
 
 0.767
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.740
Your Current Organism:
Marivirga tractuosa
NCBI taxonomy Id: 643867
Other names: Flexibacter tractuosus DSM 4126, Flexibacter tractuosus IFO 15989, M. tractuosa DSM 4126, Marivirga tractuosa DSM 4126, Marivirga tractuosa IFO 15989, Marivirga tractuosa str. DSM 4126, Marivirga tractuosa strain DSM 4126
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