The bacterial phosphoenolpyruvate (PEP)-phosphotransferase system (PTS) is widely found in bacteria, fungi and some archaea, but not in plants and animals. PTS is composed of phosphotransferases such as enzyme I (EI), histidine phosphate carrier protein (HPr or NPr), and enzyme II complex. It has both a catalytic transport function and a very extensive regulatory function. PTS mainly phosphorylates various sugars and their derivatives through a phosphate cascade and then transports them into the cell. It not only participates in the metabolism of carbon and nitrogen sources, regulates the homeostasis of iron and potassium, regulates the virulence of certain pathogens, but it also mediates stress responses. During these different regulatory processes, the signal is provided by the phosphorylation state of the PTS components, which changes according to the availability of the PTS substrate and the metabolic state of the cell. This article reviews the composition and regulatory network of phosphotransferase systems in bacteria, with a goal to provide a knowledge base for the study of the overall regulatory mechanism of the PTS and its effect on the overall metabolism of bacteria.