General Information

    • DRAMP ID

    • DRAMP18223

    • Peptide Name

    • Sonorensin(Bacteriocin)

    • Source

    • Bacillus sonorensis MT93

    • Family

    • Belongs to the class I bacteriocin

    • Gene

    • Not found

    • Sequence

    • CWSCMGHSCWSCMGHSCWSCAGHSCWSCMGHSCWSCMGHSCWSCAGHCCGSCWHGGM

    • Sequence Length

    • 57

    • Protein Existence

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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP18223 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18223.

Physicochemical Information

    • Formula

    • C249H338N78O70S20

    • Absent Amino Acids

    • DEFIKLNPQRTVY

    • Common Amino Acids

    • C

    • Mass

    • 6185.1

    • PI

    • 7.11

    • Basic Residues

    • 7

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +7

    • Boman Index

    • -1408

    • Hydrophobicity

    • 0.153

    • Aliphatic Index

    • 3.51

    • Half Life

      • Mammalian:1.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 39375

    • Absorbance 280nm

    • 703.13

    • Polar Residues

    • 36

DRAMP18223

DRAMP18223 chydropathy plot

Comments Information

    • The Clustal W alignment of the N terminus of sonorensin revealed homology with the leader sequences of protoxins from various Bacillus strains. This indicated that sonorensin, produced initially as a protoxin, was posttransitionally modified to active bacteriocin. The purified sonorensin was also found to be heat stable, stable at low temperature, biologically active over a wide pH range, and not affected in the presence of organic solvents, surfactants, and reducing agents. However, sonoresin was protease-sensitive.

Literature Information

  • ·Literature 1

    • Title

    • Sonorensin: an antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93.

    • Reference

    • Appl Environ Microbiol. 2014 May;80(10):2981-90.

    • Author

    • Chopra L, Singh G, Choudhary V, Sahoo DK.