v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [ , , ]; subtilin biosynthesis protein SpaC from Bacillus subtilis [, ]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis []; nisin biosynthesis protein NisC from Lactococcus lactis [, , ]; GCR2 from Arabidopsis thaliana []; and many others. The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution [ ]. The globular structure is characterised by an all-α fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hydrophobic periodicity has led several authors to claim various members of the family, including eukaryotic LanC-1 and GCR2, to be novel G protein-coupled receptors [, ]; some of these claims have since been corrected [, , ]. This entry represents Nisin biosynthesis protein NisC [ , , ] is believed to be involved in the cyclisation of the lantibiotic nisin: specifically, nisin contains 5 cyclic thioethers, which are installed by the NisC enzyme. |
| Short Name | Nisin_biosynthesis_NisC |