LANC_like

Lanthionine synthetase C-like protein
LANC_like
SMART accession number:SM01260
Description: Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs (PUBMED:11376939). Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains (PUBMED:12127987). This region contains seven internal repeats.
Interpro abstract (IPR007822):

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) [(PUBMED:11474189), (PUBMED:10944443), (PUBMED:12566319)]; subtilin biosynthesis protein SpaC from Bacillus subtilis [(PUBMED:1735728), (PUBMED:1539969)]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis [(PUBMED:1740156)]; nisin biosynthesis protein NisC from Lactococcus lactis [(PUBMED:8161176), (PUBMED:7689965), (PUBMED:1482192)]; GCR2 from Arabidopsis thaliana [(PUBMED:17347412)]; and many others.

The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution [(PUBMED:16527981)]. The globular structure is characterised by an all-alpha fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hyrophobic 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 [(PUBMED:17347412), (PUBMED:9512664)]; some of these claims have since been corrected [(PUBMED:10944443), (PUBMED:18086512), (PUBMED:17894782)].

The C terminus of the lantibiotic biosynthesis protein LanM is homologous to LanC [(PUBMED:19393544), (PUBMED:23071302)].

Family alignment:
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There are 8676 LANC_like domains in 8665 proteins in SMART's nrdb database.

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