v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Lantibiotics are peptide antimicrobials characterized by the unique amino acids lanthionine and methyllanthionine, which are introduced by dehydration of Ser/Thr residues and linkage of the resulting dehydrated amino acids with Cys residues. Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis [ ]. This catalysis by LanM distinguishes the type 2 lantibiotics, such as lacticin 481, mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin.The N-terminal domain of LanM enzymes contains regions associated with Ser and Thr dehydration [ ]. The C-terminal region is a LanC-type domain () that catalyses the formation of the lanthionine bridge [ ]. In most lantibiotic-producing bacteria LanM modifies only a single lantibiotic precursor peptide. However, marine Prochlorococcus and Synechococcus contain multiple lantipeptide precursor lanA-like genes but only a single lanM-like gene [ ]. |
| Short Name | Lanti_2_LanM |