Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator.

ABSTRACT: Phosphorylation of proteins is a key component of bacterial signaling systems that can control important functions such as community development and virulence. We report here the identification of a Ubiquitous bacterial Kinase (UbK) family member, designated UbK1, in the anaerobic periodontal pathogen, Porphyromonas gingivalis. UbK1 contains conserved SPT/S, Hanks-type HxDxYR, EW, and Walker A motifs, and a mutation analysis established the Walker A domain and the Hanks-type domain as required for both autophosphorylation and transphosphorylation. UbK1 autophosphorylates on the proximal serine in the SPT/S domain as well as the tyrosine residue within the HxDxYR domain and the tyrosine residue immediately proximal, indicating both serine/threonine and tyrosine specificity. The orphan two-c

SUBMITTER: Perpich JD 

PROVIDER: S-EPMC8440399 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature