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
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co-expression
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[Homology]
Score
VC_0977Conserved hypothetical protein; Identified by Glimmer2; putative. (306 aa)    
Predicted Functional Partners:
VC_0186
Glutathione reductase; Similar to SP:P06715 GB:M13141 PID:146248 PID:466637 GB:U00096; identified by sequence similarity; putative.
  
 
 0.965
hslU
Protease 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.
  
 
 0.925
hslV
Protease HslVU, subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.923
grpE
Heat shock protein GrpE; 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- [...]
  
  
 0.913
groL1
Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.879
groL2
Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.879
htpG
Heat shock protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family.
  
 
 0.869
trxB
Thioredoxin reductase; Similar to GB:J03762 SP:P09625 PID:148073 PID:347239 GB:U00096; identified by sequence similarity; putative.
  
 
 0.833
VC_2696
fxsA protein; Similar to GB:U14003 SP:P37147 GB:X04066 PID:41007 PID:536984; identified by sequence similarity; putative.
   
    0.811
dnaJ
dnaJ 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 DnaJ, DnaK and Gr [...]
  
 
 0.770
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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