Prediction of prkC-mediated protein serine/threonine phosphorylation sites for bacteria.

ABSTRACT: As an abundant post-translational modification, reversible phosphorylation is critical for the dynamic regulation of various biological processes. prkC, a critical serine/threonine-protein kinase in bacteria, plays important roles in regulation of signaling transduction. Identification of prkC-specific phosphorylation sites is fundamental for understanding the molecular mechanism of phosphorylation-mediated signaling. However, experimental identification of substrates for prkC is time-consuming and labor-intensive, and computational methods for kinase-specific phosphorylation prediction in bacteria have yet to be developed. In this study, we manually curated the experimentally identified substrates and phosphorylation sites of prkC from the published literature. The analyses of the sequenc

SUBMITTER: Zhang QB 

PROVIDER: S-EPMC6168130 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature