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
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gene neighborhood
gene co-occurrence
gene fusions
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hslUATP-dependent hsl 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. (488 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 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- [...]
  
  
 0.926
groL
Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.912
groS
Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.898
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
   
  
 0.898
lon
ATP-dependent protease LaType I; 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.
  
  
 0.816
lon-2
ATP-dependent protease LaType I; 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.
  
  
 0.816
AHC16405.1
33 kDa chaperonin.
   
  
 0.799
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.746
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 
 
0.721
Your Current Organism:
Salinispira pacifica
NCBI taxonomy Id: 1307761
Other names: DSM 27196, JCM 18663, S. pacifica, Salinispira pacifica Ben Hania et al. 2015, Spirochaeta sp. L21-RPul-D2, strain L21-RPul-D2
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