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
EDS73972.1Hsp20/alpha crystallin family protein; KEGG: tpv:TP04_0470 0.0014 lysyl-tRNA synthetase K01871; COG: COG0071 Molecular chaperone (small heat shock protein). (138 aa)    
Predicted Functional Partners:
clpB
Putative ATP-dependent chaperone protein 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.
  
 
 0.672
EDS74020.1
ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family.
  
 
 0.672
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 
 0.597
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 [...]
  
 
 0.527
EDS74568.1
DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65.
  
 
 0.527
EDS75520.1
Kinase domain protein; KEGG: lmo:lmo1820 5.3e-110 similar to putative serine/threonine-specific protein kinase K08884; COG: COG2815 Uncharacterized protein conserved in bacteria; Psort location: CytoplasmicMembrane, score: 9.49.
  
 
 0.517
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.504
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.504
grpE
Co-chaperone 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-depend [...]
  
  
 0.491
EDS73969.1
PSP1 C-terminal domain protein; COG: COG1774 Uncharacterized homolog of PSP1; Psort location: Cytoplasmic, score: 8.87.
  
    0.486
Your Current Organism:
Clostridium spiroforme
NCBI taxonomy Id: 428126
Other names: Clostridium spiroforme ATCC 29900, [. spiroforme DSM 1552, [Clostridium] spiroforme DSM 1552
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.