General Information

    • DRAMP ID

    • DRAMP00060

    • Peptide Name

    • Bacteriocin cinnamycin (Lanthiopeptin Ro 09-0198)

    • Source

    • Streptomyces cinnamoneus cinnamoneus DSM 40005 (Gram-positive bacteria)

    • Family

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

    • Gene

    • cinA

    • Sequence

    • CRQSCSFGPFTFVCDGNTK

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antbacterial, Antiviral

    • Target Organism

    • Bacillus, herpes simplex virus.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • phosphatidylethanolamine

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

    • Beta strand (2 strands; 2 residues)

    • Structure Description

    • The peptide has a hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanolamine head group would be unable to fit the pocket.

    • Helical Wheel Diagram

    • DRAMP00060 helical wheel diagram

    • PDB ID

    • 2DDE resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP00060.

Physicochemical Information

    • Formula

    • C89H133N25O28S3

    • Absent Amino Acids

    • AEHILMWY

    • Common Amino Acids

    • CF

    • Mass

    • 2097.37

    • PI

    • 7.96

    • Basic Residues

    • 2

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 4

    • Net Charge

    • +1

    • Boman Index

    • -34.61

    • Hydrophobicity

    • -0.221

    • Aliphatic Index

    • 15.26

    • Half Life

      • Mammalian:1.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 6.94

    • Polar Residues

    • 10

DRAMP00060

DRAMP00060 chydropathy plot

Comments Information

    • Function

    • Can act as inhibitor of the enzyme phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. Its antimicrobial activities are not very pronounced.

    • PTM

    • Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.

Literature Information

  • ·Literature 1

    • Title

    • Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin.

    • Reference

    • J Antibiot (Tokyo). 1990 Nov;43(11):1403-1412.

    • Author

    • Fredenhagen A, Fendrich G, Märki F, Märki W, Gruner J, Raschdorf F, Peter HH.
  • ·Literature 2

    • Title

    • Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin.

    • Reference

    • J Antibiot (Tokyo). 1989 Jun;42(6):837-845.

    • Author

    • Naruse N, Tenmyo O, Tomita K, Konishi M, Miyaki T, Kawaguchi H, Fukase K, Wakamiya T, Shiba T.
  • ·Literature 3

    • Title

    • Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.

    • Reference

    • J Biochem. 1996 Feb;119(2):226-230.

    • Author

    • Hosoda K, Ohya M, Kohno T, Maeda T, Endo S, Wakamatsu K.