Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.13.3 extracted from

  • Kaspar, S.; Perozzo, R.; Reinelt, S.; Meyer, M.; Pfister, K.; Scapozza, L.; Bott, M.
    The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor (1999), Mol. Microbiol., 33, 858-872.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D56N phosphorylation of CitB is inhibited by a D56N exchange. In the presence of ATP, CitB-D56N forms a stable complex with MalE-CitAC Klebsiella pneumoniae
H350L autokinase activity of CitA is abolished by an H350L exchange Klebsiella pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane CitA represents a membrane-bound sensor kinase consisting of a periplasmic domain flanked by two transmembrane helices, a linker domain and the conserved kinase or transmitter domain Klebsiella pneumoniae 16020
-

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae P52687
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CitB + ATP a fusion protein MalE-CitAC is composed of the maltose-binding protein and the CitA kinase domain shows constitutive autokinase activity and transfers the gamma-phosphate group of ATP to its cognate response regulator CitB Klebsiella pneumoniae ?
-
?

Synonyms

Synonyms Comment Organism
sensor kinase citA
-
Klebsiella pneumoniae