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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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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[Homology]
Score
Daci_0993TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ajs:Ajs_3931 thioredoxin. (318 aa)    
Predicted Functional Partners:
Daci_2356
TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: ecp:ECP_3590 glutathione reductase.
  
 
 0.929
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 [...]
 
  
 0.895
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.888
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.883
hslU
Heat shock protein HslVU, ATPase subunit HslU; 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.
  
 
 0.878
Daci_1501
Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
  
 
 0.791
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 
 0.753
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 [...]
 
 
 0.735
Daci_5364
TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: ajs:Ajs_3383 thioredoxin reductase.
  
 
 0.671
Daci_3978
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: biotin/lipoyl attachment domain-containing protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glucose-inhibited division protein A; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: aav:Aave_2464 dihydrolipoamide dehydrogenase.
  
 
 0.605
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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