• DRAMP ID

    • DRAMP00144
    • Peptide Name

    • Amylovorin-L (Lactobin-A; Amylovorin-L471; Bacteriocin)
    • Source

    • Lactobacillus amylovorus (Gram-positive bacteria)
    • Family

    • Belongs to the class IIb bacteriocin
    • Gene

    • amyL
    • Sequence

    • NRWTNAYSAALGCAVPGVKYGKKLGGVWGAVIGGVGGAAVCGLAGYVRKG
    • Sequence Length

    • 50
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • Lactobacillus helveticus ATCC 15009.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Cell membrane
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00144 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00144.
    • Formula

    • C220H348N64O58S2
    • Absent Amino Acids

    • DEFHMQ
    • Common Amino Acids

    • G
    • Mass

    • 4881.7
    • PI

    • 9.93
    • Basic Residues

    • 6
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 21
    • Net Charge

    • +6
    • Boman Index

    • 10.17
    • Hydrophobicity

    • 0.382
    • Aliphatic Index

    • 87.8
    • Half Life

      • Mammalian:1.4 hour
      • Yeast:3 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 15595
    • Absorbance 280nm

    • 318.27
    • Polar Residues

    • 22

DRAMP00144

DRAMP00144 chydropathy plot
    • Function

    • This heat stable bacteriocin inhibits the growth of closely related Lactobacillus species. It may act as a pore-forming protein, creating a channel in the cell membrane.
    • Subunit structure

    • Active lactobin is composed of two different peptides, one which is lactobin A.
    • Regions

    • Contains a transmembrane helix region.
  • ·Literature 1
    • Title

    • Characterization and production of amylovorin L471, a bacteriocin purified from Lactobacillus amylovorus DCE 471 by a novel three-step method.
    • Reference

    • Microbiology. 1999 Sep;145 (Pt 9):2559-2568.
    • Author

    • Callewaert R, Holo H, Devreese B, Van Beeumen J, Nes I, De Vuyst L.
  • ·Literature 2
    • Title

    • The lactobin A and amylovorin L471 encoding genes are identical, and their distribution seems to be restricted to the species Lactobacillus amylovorus that is of interest for cereal fermentations.
    • Reference

    • Int J Food Microbiol. 2004 Jan 1;90(1):93-106.
    • Author

    • De Vuyst L, Avonts L, Neysens P, Hoste B, Vancanneyt M, Swings J, Callewaert R.
  • ·Literature 3
    • Title

    • Isolation, purification, and amino acid sequence of lactobin A, one of the two bacteriocins produced by Lactobacillus amylovorus LMG P-13139.
    • Reference

    • Appl Environ Microbiol. 1997 Jan;63(1):13-20.
    • Author

    • Contreras BG, De Vuyst L, Devreese B, Busanyova K, Raymaeckers J, Bosman F, Sablon E, Vandamme EJ.