• DRAMP ID

    • DRAMP00039
    • Peptide Name

    • Pep5 (Bacteriocin)
    • Source

    • Staphylococcus epidermidis (Gram-positive bacteria)
    • Family

    • Belongs to the type A lantibiotic family (Class I bacteriocin)
    • Gene

    • pepA
    • Sequence

    • TAGPAIRASVKQCQKTLKATRLFTVSCKGKNGCK
    • Sequence Length

    • 34
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antimicrobial
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

      • Not found
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Lipid II
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Other Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Rich
    • Structure Description

    • Not found
    • DRAMP00039 helical wheel diagram
    • Formula

    • C153H269N49O44S3
    • Absent Amino Acids

    • DEHMWY
    • Common Amino Acids

    • K
    • Mass

    • 4184.11
    • PI

    • 11.08
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 10
    • Boman Index

    • -58.22
    • Hydrophobicity

    • -0.356
    • Aliphatic Index

    • 63.24
    • Half Life

      • Mammalian:7.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 125
    • Absorbance 280nm

    • 3.79
    • Polar Residues

    • 13

DRAMP00039

DRAMP00039 chydropathy plot
    • 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

    • Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.After proteolysis of the propeptide, the N-terminal 2,3-didehydrobutyrine hydrolyzes to 2-oxobutanoic acid, possibly spontaneously.
  • ·Literature 1
    • Title

    • Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence.
    • Reference

    • Arch Microbiol. 1989;152(1):16-19.
    • Author

    • Kaletta C, Entian KD, Kellner R, Jung G, Reis M, Sahl HG.
  • ·Literature 2
    • Title

    • Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation.
    • Reference

    • Eur J Biochem. 1995 Sep 1;232(2):478-489.
    • Author

    • Meyer C, Bierbaum G, Heidrich C, Reis M, S¼ling J, Iglesias-Wind MI, Kempter C, Molitor E, Sahl HG.