• DRAMP ID

    • DRAMP00037
    • Peptide Name

    • Nisin Z (Bacteriocin; Preclinical)
    • Source

    • Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria)
    • Family

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

    • nisZ
    • Sequence

    • ITSISLCTPGCKTGALMGCNMKTATCNCSIHVSK
    • Sequence Length

    • 34
    • Evidence code

    • Protein level
    • Biological Activity

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

      • Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc, Listeria, clostridium.
    • Hemolytic Activity

      • N/A
    • Cytotoxicity

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

    • Lipid II
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Other Modifications and Unusual Amino Acids

    • There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28).
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (1 helices; 4 residues)
    • Structure Description

    • The structure shows a novel lipid II-binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds. This cage structure provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics.
    • PDB ID

    • 1WCO resolved by NMR.
    • DRAMP00037 helical wheel diagram
    • 1WCO-> 
    • Formula

    • C141H245N41O46S7
    • Absent Amino Acids

    • DEFQRWY
    • Common Amino Acids

    • CT
    • Mass

    • 4063.98
    • PI

    • 8.51
    • Basic Residues

    • 4
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 8
    • Boman Index

    • -14.86
    • Hydrophobicity

    • 0.406
    • Aliphatic Index

    • 71.76
    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 250
    • Absorbance 280nm

    • 7.58
    • Polar Residues

    • 19

DRAMP00037

DRAMP00037 chydropathy plot
    • Function

    • Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
    • PTM

    • There are two dehydroalanines (Dha)
  • ·Literature 1
    • Title

    • Identification and characterization of the lantibiotic nisin Z, a natural nisin variant.
    • Reference

    • Eur J Biochem. 1991 Nov 1;201(3):581-584.
    • Author

    • Mulders JW, Boerrigter IJ, Rollema HS, Siezen RJ, de Vos WM.
  • ·Literature 2
    • Title

    • The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon.
    • Reference

    • DNA Seq. 1995;5(4):203-218.
    • Author

    • Immonen T, Ye S, Ra R, Qiao M, Paulin L, Saris PE.
  • ·Literature 3
    • Title

    • The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.
    • Reference

    • Nat Struct Mol Biol. 2004 Oct;11(10):963-967.
    • Author

    • Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA.