STRINGSTRING
htpG protein (Pseudoflavonifractor capillosus) - STRING interaction network
"htpG" - High temperature protein G in Pseudoflavonifractor capillosus
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpGHigh temperature protein G ; Molecular chaperone. Has ATPase activity (642 aa)    
Predicted Functional Partners:
BACCAP_02789
Heat shock protein 70 ; Acts as a chaperone (619 aa)
   
  0.976
BACCAP_01521
Heat shock protein 70 ; Acts as a chaperone (572 aa)
   
  0.968
BACCAP_03218
DnaK family protein (437 aa)
     
  0.945
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
 
 
  0.925
groS
Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (94 aa)
     
 
  0.912
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, [...] (387 aa)
     
  0.911
BACCAP_01522
DnaJ domain protein (213 aa)
     
  0.866
clpB
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 (876 aa)
   
 
  0.849
BACCAP_02681
ATPase family associated with various cellular activities (AAA) (837 aa)
   
 
  0.849
BACCAP_02324
ATPase family associated with various cellular activities (AAA) (858 aa)
   
 
  0.849
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacillus capillosus, Bacteroides capillosus, Bacteroides capillosus ATCC 29799, P. capillosus, P. capillosus ATCC 29799, Pseudobacterium capillosum, Pseudoflavonifractor, Pseudoflavonifractor Carlier et al. 2010, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799, Ristella capillosa
Server load: low (9%) [HD]