All domains of life utilize protein phosphorylation as a mechanism of signal transduction. In bacteria, protein phosphorylation was classically thought to be mediated exclusively by histidine kinases as part of two-component signaling systems. However, it is now well appreciated that eukaryotic-like serine/threonine kinases (eSTKs) control essential processes in bacteria. A subset of eSTKs are single-pass transmembrane proteins that have extracellular penicillin-binding-protein and serine/threonine kinase-associated (PASTA) domains which bind muropeptides. In a variety of important pathogens, PASTA kinases have been implicated in regulating biofilms, antibiotic resistance, and ultimately virulence. Although there are limited examples of direct regulation of virulence factors, PASTA kinases are critical for virulence due to their roles in regulating bacterial physiology in the context of stress. This review focuses on the role of PASTA kinases in virulence for a variety of important Gram-positive pathogens and concludes with a discussion of current efforts to develop kinase inhibitors as novel antimicrobials.

生命的所有领域都利用蛋白质磷酸化作为信号转导的机制。在细菌中，传统上认为蛋白质磷酸化仅由组氨酸激酶作为两组分信号系统的一部分来介导。但是，现在已经很清楚，真核样丝氨酸/苏氨酸激酶（eSTK）控制细菌中的基本过程。eSTK的一个子集是单程跨膜蛋白，具有跨细胞膜的青霉素结合蛋白和丝氨酸/苏氨酸激酶相关（PASTA）结构域，可以结合多肽。在多种重要的病原体中，PASTA激酶与调节生物膜，抗生素抗性和最终毒力有关。尽管直接调节毒力因子的例子有限，PASTA激酶对毒力至关重要，因为它们在压力环境下可调节细菌生理。这篇综述着重于PASTA激酶在多种重要的革兰氏阳性病原体的毒力中的作用，并以对当前开发激酶抑制剂作为新型抗微生物剂的努力进行了讨论。