Abstract
Protein phosphorylation is a key mechanism regulating cell wall synthesis in Streptococcus. Serine/threonine kinases (STKs) and the two-component system dynamically regulate peptidoglycan synthesis and assembly through phosphorylation, profoundly influencing bacterial shape maintenance, division, and drug resistance. Studies indicate that serine/threonine kinases form a core network regulating cell wall stability by phosphorylating key scaffold proteins such as DivIVA and GpsB, making them important potential targets for novel antimicrobial agents. Despite significant research progress, the spatiotemporal dynamics of this phosphorylation network and its interactions with other modification systems, such as acetylation and ubiquitination, remain to be thoroughly elucidated. Future research should integrate frontier technologies such as high-throughput proteomics and AI-based structural prediction to comprehensively elucidate this complex regulatory system, thereby providing novel strategies to address antimicrobial resistance challenges.