• DRAMP ID

    • DRAMP00195
    • Peptide Name

    • Colicin-V (Microcin-V; Bacteriocin)
    • Source

    • Escherichia coli (Gram-negative bacteria)
    • Family

    • Belongs to the class IIa microcin
    • Gene

    • cvaC
    • Sequence

    • ASGRDIAMAIGTLSGQFVAGGIGAAAGGVAGGAIYDYASTHKPNPAMSPSGLGGTIKQKPEGIPSEAWNYAAGRLCNWSPNNLSDVCL
    • Sequence Length

    • 88
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli (also closely related bacteria), Enterobacteriaceae.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Cell membrane
    • 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

    • DRAMP00195 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00195.
    • Formula

    • C381H594N108O120S4
    • Absent Amino Acids

    • ?
    • Common Amino Acids

    • GA
    • Mass

    • 8735.8
    • PI

    • 6.78
    • Basic Residues

    • 6
    • Acidic Residues

    • 5
    • Hydrophobic Residues

    • 31
    • Net Charge

    • +1
    • Boman Index

    • -49.96
    • Hydrophobicity

    • -0.003
    • Aliphatic Index

    • 74.55
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 15595
    • Absorbance 280nm

    • 179.25
    • Polar Residues

    • 36

DRAMP00195

DRAMP00195 chydropathy plot
    • Function

    • Colicin V kills sensitive cells by disrupting the membrane potential. It targets bacterial membranes and induces ion channel formation, leading to the disruption of the proton-motive force and hence ATP production.
    • PTM

    • Contains one disulfide bond between 76-87.
  • ·Literature 1
    • Title

    • Purification and characterization of colicin V from Escherichia coli culture supernatants.
    • Reference

    • Biochemistry. 1994 Jun 7;33(22):6911-6917.
    • Author

    • Fath MJ, Zhang LH, Rush J, Kolter R.
  • ·Literature 2
    • Title

    • The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by Gram-positive bacteria.
    • Reference

    • Microbiology. 1994 Sep;140 (Pt 9):2383-2389.
    • Author

    • H¥varstein LS, Holo H, Nes IF.
  • ·Literature 3
    • Title

    • Genetic analysis of an MDR-like export system: the secretion of colicin V.
    • Reference

    • EMBO J. 1990 Dec;9(12):3875-3884.
    • Author

    • Gilson L, Mahanty HK, Kolter R.