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Literature summary extracted from

  • Perraud, A.L.; Kimmel, B.; Weiss, V.; Gross, R.
    Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins (1998), Mol. Microbiol., 27, 875-887.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Bordetella pertussis P16575
-
-
2.7.13.3 Escherichia coli P30855
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 BvgA + ATP
-
 Bordetella pertussis ?
-
 ?
2.7.13.3 BvgA + ATP one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA Escherichia coli ?
-
 ?
2.7.13.3 EvgA + ATP one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA Escherichia coli ?
-
 ?

Synonyms

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