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.
Node Color
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.
Knowledge-based Evidence
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
hslVPeptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (182 aa)    
Predicted Functional Partners:
hslU
ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
 
 0.999
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- [...]
   
  
 0.903
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, [...]
   
  
 0.896
htpG
Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity.
   
  
 0.812
KGL12716.1
Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.812
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.794
lon
Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
   
  
 0.792
KGL12675.1
Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.792
KGL12437.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.772
groES
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.770
Your Current Organism:
Helicobacter muridarum
NCBI taxonomy Id: 216
Other names: ATCC 49282, CCUG 29262, CIP 104248, DSM 22221, H. muridarum, LMG 13646, LMG:13646, NCTC 12714, strain ST1
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