Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity). Flavucin has high antimicrobial activity against several pathogenic bacteria such as S.aureus, E.faecalis, E.faecium and L.monocytogenes. Is also active against the Gram-negative P.aeruginosa (PubMed:27294279). Antimicrobial activity depends on the dehydration degree and integrity of flavucin. Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. A heterologous expression system was used to produce flavucin. The gene has been fused to the leader peptide gene sequence of the model lantibiotic nisin. The construct was plugged into the nisin expression and modification machinery, and produced in L.lactis. Growth conditions that yield detectable antimicrobial activity in C.lipophiloflavum could not be identified. Belongs to the type A lantibiotic family.