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
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
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[Homology]
Score
Aave_0628KEGG: rfr:Rfer_1948 molecular chaperone, HSP70 class. (416 aa)    
Predicted Functional Partners:
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 [...]
 
 0.920
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.852
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.838
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, D [...]
 
 0.827
Aave_3228
PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like.
 
 0.819
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.801
Aave_3825
KEGG: bcn:Bcen_5665 hypothetical protein.
  
 0.738
hscB
Co-chaperone Hsc20; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.
  
 0.697
Aave_2444
FeS cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
  
 0.696
clpB
ATPase AAA-2 domain protein; 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.
  
 
 0.686
Your Current Organism:
Acidovorax citrulli
NCBI taxonomy Id: 397945
Other names: A. citrulli AAC00-1, Acidovorax avenae subsp. citrulli AAC00-1, Acidovorax citrulli AAC00-1, Acidovorax citrulli str. AAC00-1, Acidovorax citrulli strain AAC00-1
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