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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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
htpXHeat-shock protein HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. (290 aa)    
Predicted Functional Partners:
hflB
ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
  
 0.896
AMQ43127.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.767
grpE
Molecular chaperone 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 [...]
  
  
 0.762
AMQ43973.1
Hypothetical protein; Binds to the HflBKC complex which modulates FtsH activity; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the BI1 family.
  
  
 0.752
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 
 0.738
AMQ43252.1
Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.705
AMQ44437.1
FxsA protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.660
hslU
ATP-dependent protease ATP-binding 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.
   
  
 0.647
dnaJ
Molecular chaperone 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, [...]
  
 
 0.646
groES
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
  
 0.582
Your Current Organism:
Aeromonas veronii
NCBI taxonomy Id: 654
Other names: A. veronii, ATCC 35624, ATCC 49904 [[Aeromonas ichthiosmia]], Aeromonas culicicola, Aeromonas culicicola Pidiyar et al. 2002, Aeromonas hybridization group 10 (HG10), Aeromonas ichthiosmia, Aeromonas sp. G18, Aeromonas sp. R1, Aeromonas sp. R9, Aeromonas sp. TH074, Aeromonas sp. TH076, CCUG 27821, CECT 4257, CECT 4486 [[Aeromonas ichthiosmia]], CIP 103438, CIP 104613 [[Aeromonas ichthiosmia]], CIP 107763 [[Aeromonas culicicola]], DSM 6393 [[Aeromonas ichthiosmia]], DSM 7386, Enteric Group 77, JCM 7375, JCM 8354 [[Aeromonas ichthiosmia]], LMG 12645 [[Aeromonas ichthiosmia]], LMG:12645 [[Aeromonas ichthiosmia]], MTCC 3249 [[Aeromonas culicicola]], NCIMB 13205 [[Aeromonas ichthiosmia]], NICM 5147 [[Aeromonas culicicola]], strain 115/II [[Aeromonas ichthiosmia]]
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