• DRAMP ID

    • DRAMP18329
    • Peptide Name

    • Pneumococin N(Bacteriocin)
    • Source

    • Streptococcus pneumoniae?TIGR4
    • Family

    • Belongs to the class IIb bacteriocin
    • Gene

    • blpN
    • Sequence

    • NSGGAAVVAALGCAAGGVKYGRLLGPWGAAIG
    • Sequence Length

    • 32
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Biological Activity

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

    • Gram-positive
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP18329 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP18329.
    • Formula

    • C128H206N38O36S
    • Absent Amino Acids

    • DEFHMQT
    • Common Amino Acids

    • G
    • Mass

    • 2885.34
    • PI

    • 9.31
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 16
    • Net Charge

    • +2
    • Boman Index

    • 2770
    • Hydrophobicity

    • 0.791
    • Aliphatic Index

    • 100.94
    • Half Life

      • Mammalian:1.4 hour
      • Yeast:3 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 6990
    • Absorbance 280nm

    • 225.48
    • Polar Residues

    • 13

DRAMP18329

DRAMP18329 chydropathy plot
    • Comparison of the TIGR4 BlpM and -N amino acid sequences demonstrated that only ?ve amino acid differences were suf?cient to target the heterologous strain.

  • ·Literature 1
    • Title

    • The blp bacteriocins of Streptococcus pneumoniae mediate intraspecies competition both in vitro and in vivo.
    • Reference

    • Infect Immun. 2007 Jan;75(1):443-51.
    • Author

    • Dawid S, Roche AM, Weiser JN.