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Literature summary for 2.7.13.3 extracted from

  • George Cisar, E.A.; Geisinger, E.; Muir, T.W.; Novick, R.P.
    Symmetric signalling within asymmetric dimers of the Staphylococcus aureus receptor histidine kinase AgrC (2009), Mol. Microbiol., 74, 44-57.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Activating Compound

Activating Compound Comment Organism Structure
auto-inducible protein I dose-dependent activation by autoinducing peptide Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
G394A/G396A completely inactive Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + protein L-histidine Staphylococcus aureus
-
 ADP + protein N-phospho-L-histidine
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + protein L-histidine
-
 Staphylococcus aureus ADP + protein N-phospho-L-histidine
-
 ?

Subunits

Subunits Comment Organism
dimer AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide Staphylococcus aureus

Synonyms

Synonyms Comment Organism
AgrC
-
 Staphylococcus aureus
receptor histidine kinase
-
 Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Staphylococcus aureus

General Information

General Information Comment Organism
physiological function the AgrC receptor histidine kinase detects its autoinducing peptide ligand and generates an intracellular signal resulting in secretion of virulence factors Staphylococcus aureus