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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane protein | Bordetella pertussis | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bordetella pertussis | P16575 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | autophosphorylation | Bordetella pertussis |
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 | Comment | Organism |
---|---|---|
virulence sensor protein bvgS precursor | - |
Bordetella pertussis |