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Even though the biosynthetic gene cluster in charge of CTA production and the thioamide synthetase that catalyzes sulfur incorporation were recently found, the logic for peptide anchor assembly has remained a mystery. Here, with the use of in vitro biochemical assays, we indicate that the amide backbone of CTA is put together in a silly thiotemplated pathway relating to the collaboration of a transacylating member of the papain-like cysteine protease family and an iteratively acting ATP-grasp necessary p