• DRAMP ID

    • DRAMP00128
    • Peptide Name

    • Plantaricin J (PlnJ; Bacteriocin)
    • Source

    • Lactobacillus plantarum C11 (Gram-positive bacteria)
    • Family

    • Belongs to the class IIb bacteriocin
    • Gene

    • plnJ
    • Sequence

    • GAWKNFWSSLRKGFYDGEAGRAIRR
    • Sequence Length

    • 25
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial
    • Target Organism

      • Gram-positive bacteria: Pediococcus pentosaceus Pac 1.0 (MIC=50 nM), Lactobacillus plantarum 965 (MIC=0.1 nM), L. sake NCDO 2714 (MIC=50 nM), Leptostylus viridescens NCDO 1655 (MIC=5 nM). [PlnJ:PlnK=1:1]
    • Hemolytic activity

    • Unknown
    • Binding Traget

    • Unknow
    • Structure

    • Alpha helix
    • Structure Description

    • In DPC micelles, PlnJ has an N-terminal amphiphilic alpha-helix between Trp-3 and Tyr-15. Crucial residues: Gly-13 in PlnJ is very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. Gly-20 in PlnJ was replaced, the activity was reduced less than 10-fold.
    • DRAMP00128 helical wheel diagram
    • 2KHF-> 
    • Formula

    • C133H198N42O34
    • Absent Amino Acids

    • CHMPQTV
    • Common Amino Acids

    • GR
    • Mass

    • 3357.55
    • PI

    • 11.51
    • Basic Residues

    • 6
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 9
    • Boman Index

    • -70.24
    • Hydrophobicity

    • -93.2
    • Aliphatic Index

    • 43.2
    • Half Life

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

    • 12490
    • Absorbance 280nm

    • 520.42
    • Polar Residues

    • 8

DRAMP00128

DRAMP00128 chydropathy plot
    • A 1

    • 1 ratio of PlnK and PlanJ is at least 1000 times more active than the individual peptide.
  • Literature 1
    • Reference

    • Appl Environ Microbiol. 1998 Jun;64(6):2269-2272.
    • Author

    • Anderssen EL, Diep DB, Nes IF, Eijsink VG, Nissen-Meyer J.
    • Title

    • Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A.
  • Literature 2
    • Reference

    • Peptides. 2009 Sep;30(9):1613-1621.
    • Author

    • Rogne P, Haugen C, Fimland G, Nissen-Meyer J, Kristiansen PE.
    • Title

    • Three-dimensional structure of the two-peptide bacteriocin plantaricin JK.