• DRAMP ID

    • DRAMP18320
    • Peptide Name

    • Epilancin 15X(Bacteriocin)
    • Source

    • Staphylococcus epidermidis 15X154
    • Family

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

    • Not found
    • Sequence

    • SASIVKTTIKASKKLCRGFTLTCGCHFTGKK
    • Sequence Length

    • 31
    • Protein Existence

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+
    • Target Organism

    • Gram-positive
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Non helix or strand structure
    • Structure Description

    • The peptide was found to highly resemble the previously identified epilancin K7 with 68% sequence identity, three nearly identical lanthionine rings and a modified amino acid at the N-terminus. The C-terminal B and C rings of epilancin 15X are structurally similar to the D and E rings of nisin A that are believed to be involved in pore formation.
    • Helical Wheel Diagram

    • DRAMP18320 helical wheel diagram
    • PDB ID

    • 1W9N resolved by NMR
    • Predicted Structure

    • There is no predicted structure for DRAMP18320.
    • Formula

    • C145H248N42O40S3
    • Absent Amino Acids

    • DEMNPQWY
    • Common Amino Acids

    • K
    • Mass

    • 3316
    • PI

    • 10.07
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +8
    • Boman Index

    • -3597
    • Hydrophobicity

    • -0.023
    • Aliphatic Index

    • 66.13
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 125
    • Absorbance 280nm

    • 4.17
    • Polar Residues

    • 14

DRAMP18320

DRAMP18320 chydropathy plot
    • The compound contains an unusual N-terminal D-lactate group that could be essential for biological activity. This study demonstrates that this moiety confers stability against proteolytic degradation by aminopeptidases.

  • ·Literature 1
    • Title

    • Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis.
    • Reference

    • FEBS Lett. 2005 Mar 28;579(9):1917-22.
    • Author

    • Ekkelenkamp MB, Hanssen M, Danny Hsu ST, de Jong A, Milatovic D, Verhoef J, van Nuland NA.
  • ·Literature 2
    • Title

    • Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate.
    • Reference

    • Chem Biol. 2011 Jul 29;18(7):857-67.
    • Author

    • Vel