Regulation of yersinia protein kinase A (YpkA) Kinase activity by Multisite autophosphorylation and identification of an n-terminal substrate-binding domain in YpkA

Abstract

Background: The catalytic mechanism of the Yersinia protein kinase YpkA is poorly understood. Results: Multiple N-terminal autophosphorylation sites regulate YpkA activation and residues 40-49 of YpkA contribute to Gαq binding and phosphorylation. Conclusion: The N-terminal domain of YpkA plays a role in autophosphorylation and substrate binding. Significance: Elucidating how type III bacterial effectors are regulated is essential to our understanding of infectious diseases.