STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hslOConserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. (293 aa)    
Predicted Functional Partners:
ftsH
Conserved hypothetical protein; 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.
  
  
 0.858
ABD29634.1
Conserved hypothetical protein.
  
  
 0.828
ABD29641.1
Conserved hypothetical protein; Belongs to the cysteine synthase/cystathionine beta- synthase family.
       0.714
hslV
Heat shock protein HslV, putative; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.648
hslU
Heat shock protein 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.
   
  
 0.638
grpE
Co-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-depend [...]
   
  
 0.635
tilS
Conserved hypothetical protein; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
       0.629
ABD29638.1
Hypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
       0.629
groS
Chaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.625
dnaK
DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
  
 0.590
Your Current Organism:
Staphylococcus aureus
NCBI taxonomy Id: 93061
Other names: S. aureus subsp. aureus NCTC 8325, Staphylococcus aureus NCTC 8325, Staphylococcus aureus subsp. aureus NCTC 8325, Staphylococcus aureus subsp. aureus str. NCTC 8325, Staphylococcus aureus subsp. aureus strain NCTC 8325
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