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
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Neighborhood
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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
Rta_28350Chaperone protein-like protein. (422 aa)    
Predicted Functional Partners:
grpE
Candidate heat shock protein, HSP70 cofactor; 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. S [...]
  
 0.934
htpG
Candidate heat shock protein, HSP90 family; Molecular chaperone. Has ATPase activity.
   
 0.926
groL
groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.906
Rta_16570
Hypothetical protein.
  
 0.865
dnaJ
Candidate heat shock protein J; 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 [...]
  
 0.865
groS
groES protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.850
lysU
Candidate lysyl-tRNA synthetase (Lysine--tRNA ligase); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.846
clpA
Candidate ATP-dependent Clp protease ATP-binding subunit clpA; Belongs to the ClpA/ClpB family.
  
 
 0.844
clpB
Candidate heat shock 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.
  
 
 0.844
iscU
Candidate Fe-S cluster assembly protein; 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.
  
 0.806
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
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