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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
htpGChaperone protein HtpG; Molecular chaperone. Has ATPase activity. (625 aa)    
Predicted Functional Partners:
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, [...]
 
 0.979
groEL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.978
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.978
ABC0680
Molecular chaperone HscC; Belongs to the heat shock protein 70 family.
  
 0.959
ABC0679
Conserved hypothetical protein.
  
 0.932
groES
Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.905
clpQ
ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.857
acuC
Acetoin utilization protein AcuC.
    
 0.846
clpY
ATP-dependent protease HslVU (ClpYQ) ATPase subunit; 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.
   
  
 0.836
ppiB
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
 
 0.828
Your Current Organism:
Bacillus clausii
NCBI taxonomy Id: 66692
Other names: B. clausii KSM-K16, Bacillus clausii KSM-K16, Bacillus sp. (strain KSM-K16), Bacillus sp. KSM-K16
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.