General Information

    • 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

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

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

    • 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

    • Lipid II

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal 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.

    • Helical Wheel Diagram

    • DRAMP00037 helical wheel diagram

    • PDB ID

    • 1WCO resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP00037.

Physicochemical Information

    • Formula

    • C141H245N41O46S7

    • Absent Amino Acids

    • DEFQRWY

    • Common Amino Acids

    • CT

    • Mass

    • 3475.16

    • PI

    • 8.78

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +4

    • 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

Comments Information

    • 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 Information

  • ·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.