General Information

    • 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

Activity Information

    • 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

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

    • 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

    • There is no predicted structure for DRAMP18262.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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