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Literature summary for 2.7.13.3 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

Organism UniProt Comment Textmining
Bordetella pertussis P16575
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Escherichia coli P30855
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
BvgA + ATP
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Bordetella pertussis ?
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?
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 ?
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?
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 ?
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?

Synonyms

Synonyms Comment Organism
sensor protein evgS precursor
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Escherichia coli
virulence sensor protein bvgS precursor
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Bordetella pertussis