General Information

    • DRAMP ID

    • DRAMP18249

    • Peptide Name

    • Bac-GM100 (Bacteriocin)

    • Source

    • Brevibacillus brevis strain GM100

    • Family

    • Belongs to the class IId bacteriocin

    • Gene

    • Not found

    • Sequence

    • DWTFANWSCLVCDDCSVNLTV

    • Sequence Length

    • 21

    • UniProt Entry

    • No entry found

    • Protein Existence

    • SMILES

    • Not available

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

    • Not found

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C104H151N25O34S3

    • Absent Amino Acids

    • EGHIKMPQRY

    • Common Amino Acids

    • CDV

    • Mass

    • 2391.67

    • PI

    • 3.42

    • Basic Residues

    • 0

    • Acidic Residues

    • 3

    • Hydrophobic Residues

    • 9

    • Net Charge

    • -3

    • Boman Index

    • -1613

    • Hydrophobicity

    • 0.476

    • Aliphatic Index

    • 83.33

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 11125

    • Absorbance 280nm

    • 556.25

    • Polar Residues

    • 9

DRAMP18249

Comments Information

    • The 21 N-terminal residues of Bac-GM100 displayed 65% homology with thurincin H from Bacillus thuringiensis. Bac-GM100 was extremely heat-stable and was stable within a pH range of 3-10. It proved sensitive to various proteases.

Literature Information

  • ·Literature 1

    • Title

    • Purification and biochemical characterization of a highly thermostable bacteriocin isolated from Brevibacillus brevis strain GM100.

    • Reference

    • Biosci Biotechnol Biochem. 2013;77(1):151-60.

    • Author

    • Ghadbane M, Harzallah D, Laribi AI, Jaouadi B, Belhadj H.