Leucine responsive regulatory protein (Lrp) is an important transcriptional regulator in prokaryotes, which is mainly composed of conserved N-terminal DNA binding domain and C-terminal domain responding ligand, and it is widely distributed in bacteria and archaea. The C-terminal can respond to some small molecular compounds besides amino acids, and converts signals into responses by fine-tuning the spatial distribution of DNA binding domains, conformation and oligomerization of protein. Lrp can be a global or local transcription regulator to control amino acid metabolism, pili formation, heavy metal transport, polypeptide transportation, energy metabolism and other important physiological processes in microorganisms. It can also act as a "feast/famine" regulatory protein to assist microorganisms to adapt to the changeable environment. Recently, it has been found that Lrp in Actinomycetes has a universal regulation effect on antibiotic biosynthesis. In this paper, the distribution, structural characteristics, ligand categories and response modes, regulatory mechanisms, and biological functions of Lrp in bacteria and archaea were comprehensively and systematically elaborated in order to provide guidance for further study of the molecular mechanism of Lrp.