Post-translational modifications via serine/threonine phosphorylation and GpsB in <i>Streptococcus mutans</i>.

ABSTRACT: Post-translational modifications (PTMs), such as protein phosphorylation, are critical regulators of bacterial physiology. Here, we present the first comprehensive phosphoproteomic analysis of Streptococcus mutans, revealing extensive O-phosphorylation under nonstressed conditions. Using tandem mass tag (TMT)-based mass spectrometry and phosphopeptide enrichment, we identified 231 high-confidence phosphosites on 131 proteins, representing approximately 6.7% of the detected proteome. These phosphorylated proteins were enriched in pathways related to translation, carbohydrate metabolism, and the cell cycle, suggesting a broad role for O-phosphorylation in core cellular functions. To define the functional roles of the sole serine/threonine protein kinase (PknB) and phosph

SUBMITTER: Chudal S 

PROVIDER: S-EPMC12625713 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature