• DRAMP ID

    • DRAMP00012
    • Peptide Name

    • Lantibiotic lichenicidin VK21 A1 (LchA1; Lchalpha; Bacteriocin)
    • Source

    • Bacillus licheniformis (strain ATCC 14580/VK21/DSM 13) (Gram-positive bacteria)
    • Family

    • Belongs to the lantibiotic family (Class I bacteriocin)
    • Gene

    • lchA1
    • Sequence

    • TITLSTCAILSKPLGNNGYLCTVTKECMPSCN
    • Sequence Length

    • 32
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial
    • Target Organism

      • Only Lchalpha: Bacillus megaterium VKM41 (IC50=1.8 uM), Bacillus subtilis L1 (IC50=9 uM), Rhodococcus sp. SS2 (IC50=9 uM), Micrococcus luteus B1314 (IC50=1.2 uM), Staphylococcus aureus 209p (IC50=3.1 uM).
      • Lchalpha+Lchbeta: Bacillus megaterium VKM41 (IC50=0.12 uM), Bacillus subtilis L1 (IC50=0.64 uM), Rhodococcus sp. SS2 (IC50=0.64 uM), Micrococcus luteus B1314 (IC50=0.09 uM), Staphylococcus aureus 209p (IC50=0.64 uM).
    • Binding Traget

    • Cell membrane
    • Structure

    • Alpha helix (1 helices; 3 residues)
    • Structure Description

    • The Lchalpha peptide displays structural homology with mersacidin-like lantibiotics and involves relatively well-structured N- and C-terminal domains connected by a flexible loop stabilized by a thioether bridge Ala11-S-Ala21.
    • PDB ID

    • 2KTN resolved by NMR.
    • DRAMP00012 helical wheel diagram
    • 2KTN-> 
    • Formula

    • C142H239N37O47S5
    • Absent Amino Acids

    • DFHQRW
    • Common Amino Acids

    • T
    • Mass

    • 3930.11
    • PI

    • 7.91
    • Basic Residues

    • 2
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 8
    • Boman Index

    • -16.3
    • Hydrophobicity

    • 28.44
    • Aliphatic Index

    • 85.31
    • Half Life

      • Mammalian:7.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 1740
    • Absorbance 280nm

    • 56.13
    • Polar Residues

    • 18
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Amino Acid Distribution

DRAMP00012 chydropathy plot
    • Function

    • The mature peptides, Lchalpha and Lchbeta, interact synergistically to possess antibiotic activity against Gram-positive bacteria within a nanomolar concentration range, though the individual peptides were shown to be active at micromolar concentrations. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin.
    • PTM

    • Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
  • Literature 1
    • Reference

    • Appl Environ Microbiol. 2009 Sep;75(17):5451-5460.
    • Author

    • Begley M, Cotter PD, Hill C, Ross RP.
    • Title

    • Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins.
  • Literature 2
    • Reference

    • PLoS One. 2009 Aug 26;4(8):e6788.
    • Author

    • Dischinger J, Josten M, Szekat C, Sahl HG, Bierbaum G.
    • Title

    • Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13.
  • Literature 3
    • Reference

    • Biochemistry. 2010 Aug 3;49(30):6462-6472.
    • Author

    • Shenkarev ZO, Finkina EI, Nurmukhamedova EK, Balandin SV, Mineev KS, Nadezhdin KD, Yakimenko ZA, Tagaev AA, Temirov YV, Arseniev AS, Ovchinnikova TV.
    • Title

    • Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.