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Significance Lanthipeptides represent one of the largest classes of peptide natural products with a ribosomal origin, and their maturation requires a designated protease(s) to remove the N-terminal leader peptides after core peptide modifications are properly installed. For class III lanthipeptides, the identity of the protease(s) responsible for leader processing remains unclear, posing a major obstacle to their heterologous production and bioengineering. This study reveals that an unprecedented class of bifunctional Zn-dependent proteases is universally responsible for the leader removal of class III lanthipeptides, thereby clarifying the long-standing question regarding the biosynthesis of this emerging group of natural products. Our study should facilitate the discovery and bioengineering of class III lanthipeptides in the future.

Zn-dependent bifunctional proteases are responsible for leader peptide processing of class III lanthipeptides