General Information

    • DRAMP ID

    • DRAMP00056

    • Peptide Name

    • Bacteriocin ancovenin

    • Source

    • Streptomyces sp. A647P-2 (Gram-positive bacteria)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • CVQSCSFGPLTWSCDGNTK

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial

    • Target Organism

    • No MICs found in DRAMP database

    • 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

    • DRAMP00056 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP00056.

Physicochemical Information

    • Formula

    • C85H129N23O29S3

    • Absent Amino Acids

    • AEHIMRY

    • Common Amino Acids

    • CS

    • Mass

    • 2033.28

    • PI

    • 5.82

    • Basic Residues

    • 1

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 4

    • Net Charge

    • 0

    • Boman Index

    • -21.8

    • Hydrophobicity

    • -0.168

    • Aliphatic Index

    • 35.79

    • Half Life

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

    • Extinction Coefficient Cystines

    • 5625

    • Absorbance 280nm

    • 312.5

    • Polar Residues

    • 11

DRAMP00056

DRAMP00056 chydropathy plot

Comments Information

    • MOA

    • Acts as an inhibitor of angiotensin I converting enzyme.

    • 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

    • The structure of ancovenin, a new peptide inhibitor of angiotensin I converting enzyme.

    • Reference

    • Tetrahedron Lett. 1985;26:665-668.

    • Author

    • Wakamiya T, Ueki Y, Shiba T, Kido Y, Motoki Y.