Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (By similarity). Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is not secreted to influence other bacteria (Probable). Down-regulated under nitrogen starvation. Cross-links are proved in vitro, when coepressed in E.coli with the ProcM lanthionine synthetase. The lanthionine residue has both a DL configuration (with 2S,6R stereochemistry) and a LL configuration (with 2R,6R stereochemistry) (PubMed:22574919). DL and LL diastomers have a 4:1 ratio (PubMed:22574919). It is unknown whether nonenzymatic cyclization occur, but authors favor a model in which ProcM does generate all thioether cross-links (Probable). The beta-methyllanthionine residue has a DL configuration (with 2S,3S,6R stereochemistry) (PubMed:22574919). Maturation of prochlorosin involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteines. This is followed by membrane translocation and cleavage of the modified precursor.