• DRAMP ID

    • DRAMP18263
    • Peptide Name

    • Enterocin W alpha(Bacteriocin)
    • Source

    • Enterococcus faecalis NKR-4-1
    • Family

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

    • Not found
    • Sequence

    • KCPWWNLSCHLGNDGKICTYSHECTAGCNA
    • Sequence Length

    • 30
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Biological Activity

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

    • Gram-positive (Narrow)
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Cell membrane
    • 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

    • Not found
    • Structure Description

    • The cysteine, serine, and threonine residues in this peptide form a disulfide bridge and 3 dehydrated residues with or without monosulfide bridges. The amino acid sequences of the prepeptides of enterocin W showed the highest identity with those of plantaricins Walpha and Wbeta (63.3 and 44.7%, respectively).
    • Helical Wheel Diagram

    • DRAMP18263 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C140H207N41O43S5
    • Absent Amino Acids

    • FMQRV
    • Common Amino Acids

    • C
    • Mass

    • 3312.73
    • PI

    • 6.88
    • Basic Residues

    • 4
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +2
    • Boman Index

    • -3569
    • Hydrophobicity

    • -0.413
    • Aliphatic Index

    • 45.67
    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 12740
    • Absorbance 280nm

    • 439.31
    • Polar Residues

    • 16

DRAMP18263

DRAMP18263 chydropathy plot
    • The two peptides acted synergistically, and their order of binding to the cell membrane was important for their inhibitory activity.

  • ·Literature 1
    • Title

    • Isolation and characterization of enterocin W, a novel two-peptide lantibiotic produced by Enterococcus faecalis NKR-4-1.
    • Reference

    • Appl Environ Microbiol. 2012 Feb;78(3):900-3.
    • Author

    • Sawa N, Wilaipun P, Kinoshita S, Zendo T, Leelawatcharamas V, Nakayama J, Sonomoto K.