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
AFM00403.1DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. (308 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.987
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. [...]
 
 
 0.935
htpG
Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.
 
 0.887
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.
  
 
 0.818
AFM01059.1
Hypothetical protein.
  
 0.816
AFL98535.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; PFAM: domain; Domain of unknown function; Pyruvate ferredoxin/flavodoxin oxidoreductase; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric.
   
 
 0.798
AFL99061.1
Thermosome subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family.
 
 0.775
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.769
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.751
AFL98860.1
ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family.
  
 
 0.741
Your Current Organism:
Desulfitobacterium dehalogenans
NCBI taxonomy Id: 756499
Other names: D. dehalogenans ATCC 51507, Desulfitobacterium dehalogenans ATCC 51507, Desulfitobacterium dehalogenans DSM 9161, Desulfitobacterium dehalogenans JW/IU-DC1, Desulfitobacterium dehalogenans str. ATCC 51507, Desulfitobacterium dehalogenans strain ATCC 51507
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