1.C.24.1.1
Class IIa bacteriocin Pediocin PA-1 precursor of 62 aas.  Class II bacteriocins are unmodified membrane-active peptides that act over a narrow spectrum of target bacteria. They bind a specific receptor protein on the membrane to form a pore, leading to membrane permeabilization and cell death. The specific receptor acts as a docking molecule, not as a structural piece of the pore, if the bacteriocin is anchored to the membrane (Ríos Colombo et al. 2019).  Pediocin-like (or class IIa) bacteriocins (PLBs) exhibit antibacterial activity against several Gram-positive bacterial strains by forming pores in the cytoplasmic membrane of target cells with a specific receptor, the mannose phosphotransferase system (man-PTS) (Zhu et al. 2022).  The N-terminal β-sheet region of pediocin PA-1 attaches to the extracellular surface of the man-PTS core domain, whereas the C-terminal half penetrates the membrane and cracks the man-PTS like a wedge.