Ribosomally synthesized and post-translationally modified peptides (RiPPs) require precise proteolytic cleavage to generate bioactive natural products, yet the diversity of serine proteases involved remains underexplored. Here, the authors identify and characterize the serine protease WprP2 from Streptomyces venezuelae NPDC049867, revealing its unique cleavage activity on precursor peptides WprA2 involved in the biosynthesis of cyclophane RiPP natural products.
- Jabal Rahmat Haedar
- Abujunaid Habib Khan
- Chin-Soon Phan