General Information

    • DRAMP ID

    • DRAMP00138

    • Peptide Name

    • Acidocin J1132 alpha peptide (Bacteriocin)

    • Source

    • Lactobacillus acidophilus JCM 1132 (Gram-positive bacteria)

    • Family

    • Belongs to the class IIb bacteriocin

    • Gene

    • Not found

    • Sequence

    • NPKVAHCASQIGRSTAWGAVSGA

    • Sequence Length

    • 23

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • Lactobacillus.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • 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

    • DRAMP00138 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP00138.

Physicochemical Information

    • Formula

    • C96H154N32O30S

    • Absent Amino Acids

    • DEFLMY

    • Common Amino Acids

    • A

    • Mass

    • 2268.54

    • PI

    • 9.51

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +3

    • Boman Index

    • -21.6

    • Hydrophobicity

    • -0.044

    • Aliphatic Index

    • 63.91

    • Half Life

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

    • Extinction Coefficient Cystines

    • 5500

    • Absorbance 280nm

    • 250

    • Polar Residues

    • 9

DRAMP00138

DRAMP00138 chydropathy plot

Comments Information

    • Comment

    • Acidocin J1132 is a pore-forming bacteriocin that creates cell membrane channels through the "barrel-stave" mechanism. Both alpha and beta had inhibitory activity, and an increase in activity by the complementary action of the two components was observed.

Literature Information

  • ·Literature 1

    • Title

    • Isolation, partial characterization, and mode of action of Acidocin J1132, a two-component bacteriocin produced by Lactobacillus acidophilus JCM 1132.

    • Reference

    • Appl Environ Microbiol. 1996 Mar;62(3):892-897.

    • Author

    • Tahara T, Oshimura M, Umezawa C, Kanatani K.