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Literature summary extracted from

  • Uhl, M.A.; Miller, J.F.
    Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay (1996), EMBO J., 15, 1028-1036.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.13.3 H1172Q mutation abolishes BvgS activity in vivo and eliminates detectable phosphorylation of BvgA in vitro. Activity of BvgS H1172Q can be restored by providing the wild-type C-terminal domain in trans Bordetella pertussis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.13.3 membrane transmembrane protein Bordetella pertussis 16020
-

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Bordetella pertussis P16575
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.3 phosphoprotein autophosphorylation Bordetella pertussis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 BvgA + ATP the phosphorylated, purified C-terminal domain alone is sufficient for phosphotransfer to BvgA Bordetella pertussis ?
-
 ?
2.7.13.3 protein + ATP autophosphorylation Bordetella pertussis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 virulence sensor protein bvgS precursor
-
 Bordetella pertussis