Type I lantibiotic biosynthesis cyclase (IPR033889)

Short name: LanC

Overlapping homologous superfamilies


Family relationships


Lantibiotics form a class of antimicrobial peptides that are ribosomally synthesized as precursor peptides and then post-translationally modified [PMID: 17046525, PMID: 16118063, PMID: 15638769, PMID: 15450492]. Lantibiotics are post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans) in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. Class I lantibiotics possess two modification enzymes, i.e. a dehydratase LanB and a cyclase LanC. Class II lantibiotics are modified by a bi-functional enzyme called LanM, which is able to perform both the dehydration and the cyclization reactions.

LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a class I lantibiotic. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. This family also contains the cyclases involved in the biosynthesis of subtilin (SpaC) [PMID: 14622008], nisin (NisC) [PMID: 16527981] and homologues.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.