Genomic loci for this biosynthetic pathway

Cluster Type From To
The following clusters are from record BGC0000520.1:
Cluster 1RiPP11069

BGC0000520, lacticin 3147 A1 / lacticin 3147 A2 biosynthetic gene cluster from Lactococcus lactis. Locus 1. Full MIBiG entry.

Chemical compounds

Compound: lacticin 3147 A1
Molecular activity: Antibacterial
Molecular target: cellular membrane

Class-specific details

Biosynthetic class(es):
RiPP subclass:
Lantipeptide (linear)

Gene cluster description

lacticin 3147 A1 / lacticin 3147 A2 (BGC0000520). Gene Cluster 1. Biosynthetic class = RiPP. GenBank AF167432, positions 1-1069. Click on genes for more information.


biosynthetic genes
transport-related genes
regulatory genes
other genes

Detailed annotation

No core peptides found.

General MIBiG information on this cluster

Complete gene cluster sequence?incomplete
Evidence for cluster-compound connection:Knock-out studies, Enzymatic assays, Heterologous expression, Sequence-based prediction
Contact for this cluster:Oscar P. Kuipers (University of Groningen)

Literature references

1. McAuliffe O et al. (1998) Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential. Appl Environ Microbiol 64(2):439-45.
2. Ryan MP et al. (1999) Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. J Biol Chem 274(53):37544-50.
3. McAuliffe O et al. (2000) Identification and overexpression of ltnl, a novel gene which confers immunity to the two-component lantibiotic lacticin 3147. Microbiology 146 ( Pt 1):129-38. doi: 10.1099/00221287-146-1-129.
4. McAuliffe O et al. (2000) Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity. Microbiology 146 ( Pt 9):2147-54. doi: 10.1099/00221287-146-9-2147.
5. McAuliffe O et al. (2001) Regulation of immunity to the two-component lantibiotic, lacticin 3147, by the transcriptional repressor LtnR. Mol Microbiol 39(4):982-93.
6. Cotter PD et al. (2006) Overproduction of wild-type and bioengineered derivatives of the lantibiotic lacticin 3147. Appl Environ Microbiol 72(6):4492-6. doi: 10.1128/AEM.02543-05.
7. Martin NI et al. (2004) Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity. Biochemistry 43(11):3049-56. doi: 10.1021/bi0362065.
8. Kuipers A et al. (2008) Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin. Appl Environ Microbiol 74(21):6591-7. doi: 10.1128/AEM.01334-08. Epub
9. Field D et al. (2013) Saturation mutagenesis of selected residues of the alpha-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity. Microb Biotechnol 6(5):564-75. doi: 10.1111/1751-7915.12041. Epub 2013
10. Suda S et al. (2012) Lacticin 3147--biosynthesis, molecular analysis, immunity, bioengineering and applications. Curr Protein Pept Sci 13(3):193-204.
11. Rea MC et al. (2011) Effect of broad- and narrow-spectrum antimicrobials on Clostridium difficile and microbial diversity in a model of the distal colon. Proc Natl Acad Sci U S A 108 Suppl 1:4639-44. doi: