• DRAMP ID

    • DRAMP18195
    • Peptide Name

    • LsbB (Bacteriocin)
    • Source

    • Lactococcus lactis subsp. lactis (Streptococcus lactis)
    • Family

    • Not found
    • Gene

    • lsbB
    • Sequence

    • MKTILRFVAGYDIASHKKKTGGYPWERGKA
    • Sequence Length

    • 30
    • Protein Existence

    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • targeting primarily lactococcal cells
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • Serum or Protease Type

    • Not available
    • Stability Data

    • Not available
    • Assay

    • Not available
    • 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

    • alpha helical
    • Structure Description

    • Structure determination by NMR spectroscopy showed that LsbB has an N-terminal alpha helix, whereas the C-terminal of the molecule remains unstructured.
    • Helical Wheel Diagram

    • DRAMP18195 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP18195.
    • Formula

    • C156H246N44O40S
    • Absent Amino Acids

    • CNQ
    • Common Amino Acids

    • K
    • Mass

    • 3410
    • PI

    • 10.12
    • Basic Residues

    • 8
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +6
    • Boman Index

    • -5095
    • Hydrophobicity

    • -0.683
    • Aliphatic Index

    • 58.67
    • Half Life

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

    • 8480
    • Absorbance 280nm

    • 292.41
    • Polar Residues

    • 9

DRAMP18195

DRAMP18195 chydropathy plot
    • The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain. Alanine substitution revealed that the tryptophan in position 25 (Trp25) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin. 

  • ·Literature 1
    • Title

    • Novel mechanism of bacteriocin secretion and immunity carried out bylactococcal multidrug resistance proteins.
    • Reference

    • J. Biol. Chem. 278:34291-34298(2003).
    • Author

    • Gajic O., Buist G., Kojic M., Topisirovic L., Kuipers O.P., Kok J.
  • ·Literature 2
    • Title

    • Defining the structure and receptor binding domain of the leaderlessbacteriocin LsbB.
    • Reference

    • J. Biol. Chem. 289:23838-23845(2014)
    • Author

    • Ovchinnikov K.V., Kristiansen P.E., Uzelac G., Topisirovic L.,Kojic M., Nissen-Meyer J., Nes I.F., Diep D.B.