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BRENDA support

Literature summary for 2.7.13.3 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

Protein Variants Comment Organism
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

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

Organism

Organism UniProt Comment Textmining
Bordetella pertussis P16575
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein autophosphorylation Bordetella pertussis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
virulence sensor protein bvgS precursor
-
Bordetella pertussis