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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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dnaJMolecular chaperone, DnaJ family; 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 betwe [...] (377 aa)    
Predicted Functional Partners:
dnaK
DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.999
grpE
GRPE 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. Several rounds of ATP-dependent i [...]
 
 
 0.958
groEL
GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.949
Atu0988
Molecular chaperone, Hsp70 family.
  
 0.878
groES
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.869
hslU
Heat shock chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
 
 0.843
ftsH
Metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
 
 
 0.833
Atu3673
Siderophore biosynthesis protein.
   
 
 0.806
rpoH
RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes.
  
 
 0.805
clpA
ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
 
 
 0.789
Your Current Organism:
Agrobacterium fabrum
NCBI taxonomy Id: 176299
Other names: A. fabrum str. C58, Agrobacterium fabrum str. C58, Agrobacterium tumefaciens (strain C58 / ATCC 33970), Agrobacterium tumefaciens (strain C58), Agrobacterium tumefaciens str. C58, Agrobacterium tumefaciens str. C58 (Cereon), Agrobacterium tumefaciens str. C58 (Dupont), Agrobacterium tumefaciens str. C58 (U. Washington), Rhizobium radiobacter str. C58 (Cereon), Rhizobium radiobacter str. C58 (Dupont), Rhizobium radiobacter str. C58 (U. Washington)
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