• DRAMP ID

    • DRAMP00213
    • Peptide Name

    • Lactocin S (Bacteriocin)
    • Source

    • Lactobacillus sakei L45 (Gram-positive bacteria)
    • Family

    • Not found
    • Gene

    • lasA
    • Sequence

    • STPVLASVAVSMELLPTASVLYSDVAGCFKYSAKHHC
    • Sequence Length

    • 37
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • Leuconostoc, Carnobacteria, Lactobacilli, Pediococci, Lactococci, Listeria monocytogenes, Listeria innocua, Staphylococcus, Bacillus cereus, Clostridium spp.
    • Hemolytic Activity

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

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Deaminated
    • C-terminal Modification

    • Cyclization between S32 and C37
    • Nonterminal Modifications and Unusual Amino Acids

    • Two lanthionines(S32-C37,S23-C28)
    • Stereochemistry

    • Mixed(D-Ala)
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00213 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00213.
    • Formula

    • C173H273N43O52S3
    • Absent Amino Acids

    • INQRW
    • Common Amino Acids

    • S
    • Mass

    • 3883.51
    • PI

    • 6.66
    • Basic Residues

    • 4
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 15
    • Net Charge

    • +2
    • Boman Index

    • -4.01
    • Hydrophobicity

    • 0.576
    • Aliphatic Index

    • 94.86
    • Half Life

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

    • 3105
    • Absorbance 280nm

    • 86.25
    • Polar Residues

    • 13

DRAMP00213

DRAMP00213 chydropathy plot
    • MOA

    • The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
    • 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
    • Title

    • Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45.
    • Reference

    • Appl Environ Microbiol. 1991 Jun;57(6):1829-1834.
    • Author

    • M¸rtvedt CI, Nissen-Meyer J, Sletten K, Nes IF.
  • ·Literature 2
    • Title

    • In vivo conversion of L-serine to D-alanine in a ribosomally synthesized polypeptide.
    • Reference

    • J Biol Chem. 1994 Nov 4;269(44):27183-27185.
    • Author

    • Skaugen M, Nissen-Meyer J, Jung G, Stevanovic S, Sletten K, Inger C, Abildgaard M, Nes IF.