• DRAMP ID

    • DRAMP03097
    • Peptide Name

    • Drosocin (Glycopeptide,insects, arthropods, invertebrates, animals)
    • Source

    • Drosophila melanogaster (Fruit fly)
    • Family

    • Belongs to the drosocin family
    • Gene

    • Dro
    • Sequence

    • GKPRPYSPRPTSHPRPIRV
    • Sequence Length

    • 19
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • 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 turns
    • Structure Description

    • The NMR data clearly indicate a difference between the glycosylated and nonglycosylated forms, i.e., in the perturbation of a turn directly adjacent to the glycosylation site.
    • Helical Wheel Diagram

    • DRAMP03097 helical wheel diagram
    • PDB ID

    • 4EZR resolved by X-ray.
    • Predicted Structure

    • There is no predicted structure for DRAMP03097.
    • Formula

    • C98H160N34O24
    • Absent Amino Acids

    • ACDEFLMNQW
    • Common Amino Acids

    • P
    • Mass

    • 2198.56
    • PI

    • 12.01
    • Basic Residues

    • 6
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 2
    • Net Charge

    • +6
    • Boman Index

    • -69.5
    • Hydrophobicity

    • -1.579
    • Aliphatic Index

    • 35.79
    • Half Life

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

    • 1490
    • Absorbance 280nm

    • 82.78
    • Polar Residues

    • 5

DRAMP03097

DRAMP03097 chydropathy plot
    • Function

    • Antibacterial peptide with strong anti-Gram-negative bacteria activity.
    • PTM

    • O-glycosylation is essential for full biological activity.
    • Tissue specificity

    • In hemolymph 6 hours after immune challenge, levels of expression increase for first 24 hours and persist for the following two weeks.
    • Developmental stage

    • Expressed in larvae and in adults.
    • Induction

    • By bacterial infection.
  • ·Literature 1
    • Title

    • Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: effects of glycosylation on solution conformation.
    • Reference

    • Biochemistry. 1999 Jan 12;38(2):705-14.
    • Author

    • McManus AM, Otvos L Jr, Hoffmann R, Craik DJ.
  • ·Literature 2
    • Title

    • A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution.
    • Reference

    • J Biol Chem. 1993 Jul 15;268(20):14893-7.
    • Author

    • Bulet P, Dimarcq JL, Hetru C, Lagueux M, Charlet M, Hegy G, Van Dorsselaer A, Hoffmann JA.
  • ·Literature 3
    • Title

    • Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides.
    • Reference

    • J Biol Chem. 1998 Mar 13;273(11):6139-6143.
    • Author

    • Mackintosh JA, Veal DA, Beattie AJ, Gooley AA.