• DRAMP ID

    • DRAMP00201
    • Peptide Name

    • Amythiamicin A/B (Bacteriocin)
    • Source

    • Amycolatopsis sp. (strain MI481-42F4 / FERM P-12739)
    • Family

    • Belongs to the thiocillin family
    • Gene

    • Unknown
    • Sequence

    • SCNCVCGVCCSCSP
    • Sequence Length

    • 14
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial , Anti-Gram+, Antimicrobial
    • Target Organism

      • Gram-positive bacteria: Staphylococcus aureus MS9610 (MIC=0.2 µg/ml), Methicillin-resistant S. aureus (MIC=0.2 µg/ml), Staphylococcus aureus FDA209P (MIC=0.1 µg/ml), Micrococcus luteus FDA16 (MIC=0.1 µg/ml), M. luteus IFO3333 (MIC=0.78 µg/ml), M. luteus PCI1001 (MIC=0.2 µg/ml), Bacillus anthracis (MIC=0.1 µg/ml), B. subtilis NRRL B-558 (MIC=0.2 µg/ml), B. subtilis PCI219 (MIC=0.2 µg/ml), B. cereus ATCC 10702 (MIC=0.1 µg/ml).
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP00201 helical wheel diagram
    • Formula

    • C48H81N15O19S6
    • Absent Amino Acids

    • ADEFHIKLMQRTWY
    • Common Amino Acids

    • C
    • Mass

    • 1596.69
    • PI

    • 5.61
    • Basic Residues

    • 0
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 2
    • Boman Index

    • -0.14
    • Hydrophobicity

    • 110.71
    • Aliphatic Index

    • 41.43
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 375
    • Absorbance 280nm

    • 28.85
    • Polar Residues

    • 11

DRAMP00201

    • Function

    • Has bacteriocidal activity against Gram-positive bacteria
    • PTM

    • Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings.
    • Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with the alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser.

    • The diketopiperazine ester in form C may be formed by cyclization and transesterification of the C-terminal dipeptide.

  • Literature 1
    • Reference

    • J Antibiot (Tokyo). 1994 Jun;47(6):668-674.
    • Author

    • Shimanaka K, Kinoshita N, Iinuma H, Hamada M, Takeuchi T.
    • Title

    • Novel antibiotics, amythiamicins. I. Taxonomy, fermentation, isolation, physico-chemical properties, and antimicrobial activity.