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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from curated databases
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
GWL_45510Thioredoxin-related transmembrane protein. (173 aa)    
Predicted Functional Partners:
dnaJ
Molecular chaperone protein; 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 Dn [...]
    
 0.914
GWL_35690
Lipoprotein.
 
 
 0.889
dsbD
Thiol:disulfide interchange transmembrane protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily.
  
 
 0.881
htpG
HSP90 family high temperature molecular chaperone G protein; Molecular chaperone. Has ATPase activity.
   
 0.877
GWL_13050
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.
    
 0.873
GWL_13060
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.
    
 0.873
dnaK
Molecular chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.864
hscA
Molecular chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 0.864
GWL_44460
Heat-shock Hsp70 protein.
  
 0.864
GWL_45520
Hypothetical protein.
   
   0.860
Your Current Organism:
Herbaspirillum sp. GW103
NCBI taxonomy Id: 1175306
Other names: H. sp. GW103
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