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.
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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
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tlpAThiol:disulfide oxidoreductase TlpA. (228 aa)    
Predicted Functional Partners:
CSIRO_1282
Putative copper metallochaperone.
 
 
 0.938
CSIRO_1317
Cytochrome c oxidase polypeptide II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
    
 
 0.919
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.911
CSIRO_3414
Alkyl hydroperoxide reductase subunit C-like protein.
  
 0.858
CSIRO_4236
Hypothetical protein.
   
 0.817
CSIRO_2871
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
 0.811
CSIRO_2872
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
 0.811
CSIRO_3384
DnaJ-like heat shock protein.
  
 
 0.777
CSIRO_0647
DnaJ-like domain-containing protein.
    
 0.746
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 [...]
    
 0.746
Your Current Organism:
Bradyrhizobiaceae bacterium SG6C
NCBI taxonomy Id: 709797
Other names: B. bacterium SG-6C, Bradyrhizobiaceae bacterium SG-6C
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