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
AFM04200.1Actin-like ATPase involved in cell morphogenesis; PFAM: Ppx/GppA phosphatase family. (1276 aa)    
Predicted Functional Partners:
AFM04233.1
Molecular chaperone of HSP90 family; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; Hsp90 protein.
   
 0.968
grpE
Molecular chaperone GrpE (heat shock 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. [...]
  
 0.920
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.875
AFM03087.1
ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); UvrB/uvrC motif; Belongs to the ClpA/ClpB family.
  
 
 0.836
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.
  
 
 0.836
AFM04371.1
Hypothetical protein.
  
 
 0.836
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.788
AFM04037.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
  
 0.788
AFM04465.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 0.788
AFM05746.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 0.788
Your Current Organism:
Bernardetia litoralis
NCBI taxonomy Id: 880071
Other names: B. litoralis DSM 6794, Bernardetia litoralis DSM 6794, Flexibacter litoralis ATCC 23117, Flexibacter litoralis DSM 6794, Flexibacter litoralis IFO 15988
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