LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Lantibiotic genes reside on the bacterial chromosome, where they cluster with genes that adapt and secrete them to the extracellular space. Many of these so-called 'pathogenicity islands' have been characterised, including the epidermin (epi) cluster in Staphylococcus epidermis, and the nisin (nis) cluster in Lactococcus lactis [ ]. The gene encoding the lantibiotic is flanked by 3 regulatory genes: 2 that are usually involved in a 2-component regulatory system, and another that cleaves the signal peptide from the precursor to produce the mature lantibiotic.This protein (usually designated with a "P"suffix - nisP, mutP, etc.) is highly conserved amongst pathogenic species, and is essential for virulence and survival of the bacterium against competitors in the host [ ]. A novel pathogenicity island in resistant Enterococcus faecalis has been sequenced. In addition to the lantibiotic Cyl gene cluster, this revealed a novel set of virulence factors involved in vancomycin resistance and pathogenicity []. Lantiobiotic (lanthionine-containing antibiotics) specific proteases are serine proteases in the subtilisin family (family S8). The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP (MEROPS identifier S08.060), from Staphylococcus, is thought to cleave matured epidermin [ ]. NsuP, a dehydratase from Streptococcus and NisP (MEROPS identifier S08.059), a membrane-anchored protease from Lactococcus, cleaves nisin []. MutP (MEROPS identifier S08.065) is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans []. |
| Short Name | Lanit_process |
