S9 Protease WprP Catalyzes Uniform and Sequential Cleavage on the Precursor Peptide in RiPP Biosynthesis
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Serine proteases in ribosomally synthesized and post-translationally modified peptides (RiPPs) catalyze the cleavage on the precursor peptides in the biosynthesis of RiPP natural products. Here, we identified an uncharacterized serine protease WprP 2 from Streptomyces venezuelae NPDC049867, encoded next to the radical SAM enzyme WprB 2 involved in the biosynthesis of cy-clophane natural products. In vitro characterization of S9 protease WprP 2 revealed that the precursor peptide WprA 2 is uniformly and sequentially cleaved. The cleavage activity of WprP 2 has not been seen in any serine proteases and expands the S9 protease in RiPP biosynthesis.
