General Information

    • DRAMP ID

    • DRAMP18261

    • Peptide Name

    • Enterocin 7B (Bacteriocin)

    • Source

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

    • Family

    • Belongs to the class IId bacteriocin

    • Gene

    • mr10B

    • Sequence

    • MGAIAKLVAKFGWPFIKKFYKQIMQFIGQGWTIDQIEKWLKRH

    • Sequence Length

    • 43

    • Protein Existence

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

    • broad-spectrum( mainly Gram-positive)

    • 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

    • DRAMP18261 helical wheel diagram

    • Predicted Structure

Physicochemical Information

    • Formula

    • C250H380N62O54S2

    • Absent Amino Acids

    • CNS

    • Common Amino Acids

    • K

    • Mass

    • 5182.27

    • PI

    • 10.22

    • Basic Residues

    • 9

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 19

    • Net Charge

    • +7

    • Boman Index

    • -2263

    • Hydrophobicity

    • -0.109

    • Aliphatic Index

    • 86.28

    • Half Life

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

    • Extinction Coefficient Cystines

    • 17990

    • Absorbance 280nm

    • 428.33

    • Polar Residues

    • 6

DRAMP18261

DRAMP18261 chydropathy plot

Comments Information

    • leaderless, i.e. no signal peptide. Although MR10B and Enterocin 7B share the same amino acid sequence, enterocin 7B is N-terminally formylated Met. Remarkably, the peptides are helical in aqueous solution. Enterocins 7A and 7B each display strong activity by themselves without their partner.

Literature Information

  • ·Literature 1

    • Title

    • Identification of an N-terminal formylated, two-peptide bacteriocin from Enterococcus faecalis 710C.

    • Reference

    • J Agric Food Chem. 2011 May 25;59(10):5602-8.

    • Author

    • Liu X, Vederas JC, Whittal RM, Zheng J, Stiles ME, Carlson D, Franz CM, McMullen LM, van Belkum MJ.
  • ·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

    • Lohans CT, Towle KM, Miskolzie M, McKay RT, van Belkum MJ, McMullen LM, Vederas JC.