• DRAMP ID

    • DRAMP18262
    • Peptide Name

    • Enterocin 7A(Bacteriocin)
    • Source

    • Enterococcus faecalis MRR 10-3; Enterococcus faecalis 710C
    • Family

    • Belongs to the class IId bacteriocin
    • Gene

    • mr10A
    • Sequence

    • MGAIAKLVAKFGWPIVKKYYKQIMQFIGEGWAINKIIDWIKKHI
    • Sequence Length

    • 44
    • Protein Existence

    • Biological Activity

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

    • Gram-positive (broad-spectrum)
    • 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

    • Helix
    • Structure Description

    • Both peptides are primarily alpha-helical, adopting a similar overall fold. The structures can be divided into three separate alpha-helical regions: the N- and C-termini are both alpha-helical, separated by a central kinked alpha-helix. The overall structures bear an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold.
    • Helical Wheel Diagram

    • DRAMP18262 helical wheel diagram
    • PDB ID

    • 2M5Z resolved by NMR
    • Predicted Structure

    • Formula

    • C251H390N60O54S2
    • Absent Amino Acids

    • CRST
    • Common Amino Acids

    • I
    • Mass

    • 5176.35
    • PI

    • 10
    • Basic Residues

    • 9
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 21
    • Net Charge

    • +7
    • Boman Index

    • 334
    • Hydrophobicity

    • 0.202
    • Aliphatic Index

    • 110.91
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 19480
    • Absorbance 280nm

    • 453.02
    • Polar Residues

    • 7

DRAMP18262

DRAMP18262 chydropathy plot
    • leaderless, i.e. no signal peptide. The amino acid sequence of enterocin 7A is identical to that of MR10A. However, enterocin 7A is N-terminally formylated. Remarkably, the peptide is helical in aqueous solution.Enterocins 7A and 7B each display strong activity by themselves without their partner.

  • ·Literature 1
    • Title

    • Characterization of antimicrobial substances produced by Enterococcus faecalis MRR 10-3, isolated from the uropygial gland of the hoopoe (Upupa epops).
    • Reference

    • Appl Environ Microbiol. 2006 Jun;72(6):4245-9.
    • Author

    • Mart
  • ·Literature 2
    • Title

    • Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide.
    • Reference

    • Biochemistry. 2013 Jun 11;52(23):3987-94.
    • Author