Protein Domain : Nisin biosynthesis protein, NisC IPR020468

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

0 Child Features

0 Gene Families

0 Genes

0 Ontology Annotations

1 Parent Features

0 Publications

USDA
InterMine logo
The Legume Information System (LIS) is a research project of the USDA-ARS:Corn Insects and Crop Genetics Research in Ames, IA.
LegumeMine || ArachisMine | CicerMine | GlycineMine | LensMine | LupinusMine | PhaseolusMine | VignaMine | MedicagoMine
InterMine © 2002 - 2022 Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, United Kingdom