General Information

    • DRAMP ID

    • DRAMP18250

    • Peptide Name

    • Laterosporulin (Bacteriocin)

    • Source

    • Brevibacillus sp. Strain GI-9

    • Family

    • Belongs to the class IId bacteriocin

    • Gene

    • laterosporulin

    • Sequence

    • MACQCPDAISGWTHTDYQCHGLENKMYRHVYAICMNGTQVYCRTEWGSSC

    • Sequence Length

    • 50

    • Protein Existence

    • SMILES

    • Not available

Activity Information

    • Biological Activity

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

    • Target Organism

    • Gram-positive, Gram-negative (broad spectrum)

    • 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

    • Beta strand

    • Structure Description

    • The crystal structure of LS at 2.0 A resolution reveals an all-bconformation of this peptide, with four beta-strands forming a twisted b-sheet. All six intrinsic cysteines are intramolecularly disulfide-bonded, with two disulfides constraining the N terminus of the peptide and the third disulfide crosslinking the extreme C terminus, resulting in the formation of a closed structure. Despite a low overall sequence similarity, LS has disul

    • PDB ID

    • 4OZK resolved by X-ray

    • Predicted Structure

Physicochemical Information

    • Formula

    • C243H360N70O75S9

    • Absent Amino Acids

    • F

    • Common Amino Acids

    • C

    • Mass

    • 5750.5

    • PI

    • 6.22

    • Basic Residues

    • 6

    • Acidic Residues

    • 4

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +2

    • Boman Index

    • -7995

    • Hydrophobicity

    • -0.442

    • Aliphatic Index

    • 41

    • Half Life

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

    • Extinction Coefficient Cystines

    • 17335

    • Absorbance 280nm

    • 353.78

    • Polar Residues

    • 23

DRAMP18250

Comments Information

    • This peptide is thermal stable, pH tolerant, and resistant to proteases. Reducing agent DTT had no effect on peptide activity or migration on gel.

Literature Information

  • ·Literature 1

    • Title

    • Identification, purification and characterization of laterosporulin, a novel bacteriocin produced by Brevibacillus sp. strain GI-9.

    • Reference

    • PLoS One. 2012;7(3):e31498. doi: 10.1371/journal.pone.0031498.

    • Author

    • Singh PK, Chittpurna, Ashish, Sharma V, Patil PB, Korpole S.
  • ·Literature 2

    • Title

    • The intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural module.

    • Reference

    • FEBS J. 2015 Jan;282(2):203-14.

    • Author

    • Singh PK, Solanki V, Sharma S, Thakur KG, Krishnan B, Korpole S.