General Information

    • DRAMP ID

    • DRAMP18242

    • Peptide Name

    • Fengycin B2 (Bacteriocin)

    • Source

    • Bacillus thuringiensis

    • Family

    • Belongs to the lipopeptides family

    • Gene

    • Not found

    • Sequence

    • EKYTEVPEYV

    • Sequence Length

    • 10

    • UniProt Entry

    • No entry found

    • Protein Existence

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal, Anti-Gram+, Anti-Gram-

    • Target Organism

    • Gram-positive, Gram-negative

    • 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

    • K2 is Orn. The C-terminal V forms an ester bond with the side chain of Y3.

    • Helical Wheel Diagram

    • DRAMP18242 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18242.

Physicochemical Information

    • Formula

    • C58H85N11O20

    • Absent Amino Acids

    • ACDFGHILMNQRSW

    • Common Amino Acids

    • E

    • Mass

    • 1256.37

    • PI

    • 4.25

    • Basic Residues

    • 1

    • Acidic Residues

    • 3

    • Hydrophobic Residues

    • 2

    • Net Charge

    • -2

    • Boman Index

    • -2075

    • Hydrophobicity

    • -1.09

    • Aliphatic Index

    • 58

    • Half Life

      • Mammalian:1 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 2980

    • Absorbance 280nm

    • 331.11

    • Polar Residues

    • 3

DRAMP18242

Comments Information

    • Fuction

    • Active against fungi C. Albicans and A.niger.

Literature Information

  • ·Literature 1

    • Title

    • Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1.

    • Reference

    • Front Microbiol. 2013 Nov 21;4:332.

    • Author

    • Roy A, Mahata D, Paul D, Korpole S, Franco OL, Mandal SM.
  • ·Literature 2

    • Title

    • Lipopeptides from the banyan endophyte, Bacillus subtilis K1: mass spectrometric characterization of a library of fengycins.

    • Reference

    • J Am Soc Mass Spectrom. 2012 Oct;23(10):1716-28. Epub 2012 Jul 31.

    • Author

    • Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P.