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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AGA69710.1Plasmid segregation actin-type ATPase ParM. (369 aa)    
Predicted Functional Partners:
AGA69528.1
Hypothetical protein.
 
 0.889
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.881
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. [...]
  
 0.877
AGA68064.1
PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
   
 0.827
htpG
Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.
   
 0.827
AGA67948.1
ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); UvrB/uvrC motif; Belongs to the ClpA/ClpB family.
  
 
 0.808
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.
  
 
 0.808
AGA69915.1
FeS cluster assembly scaffold protein NifU; PFAM: NifU-like N terminal domain.
  
 0.799
AGA69961.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
 
 0.794
AGA70626.1
Membrane protein involved in the export of O-antigen and teichoic acid; PFAM: Polysaccharide biosynthesis protein.
  
   
 0.791
Your Current Organism:
Desulfitobacterium dichloroeliminans
NCBI taxonomy Id: 871963
Other names: D. dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans DCA1, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfitobacterium dichloroeliminans LMG P21439, Desulfitobacterium dichloroeliminans str. LMG P-21439, Desulfitobacterium dichloroeliminans strain LMG P-21439
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