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
ABD29913.1Conserved hypothetical protein. (479 aa)    
Predicted Functional Partners:
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
   
 0.899
dnaK
DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.869
hprK
HPr(Ser) kinase/phosphatase; Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable car [...]
       0.856
lgt
Prolipoprotein diacylglyceryl transferase; Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins.
       0.856
ABD29912.1
Conserved hypothetical protein.
       0.856
arcR
Conserved hypothetical protein; Positively regulates the expression of the arcABDCR operon under anaerobic conditions, by binding to the consensus motif 5'- TGTGAN(6)TCACA-3', thus playing an essential role in arginine catabolism. May also control the expression of genes encoding proteins which are involved in anaerobic metabolism. Can bind cyclic AMP.
  
 
 
 0.830
rpoZ
Conserved hypothetical protein; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
 
  0.829
betA
Choline dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate.
    
 0.828
icaA
Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity).
  
 
 0.820
rpoA
DNA-directed RNA polymerase alpha chain, putative; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 0.811
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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.