• DRAMP ID

    • DRAMP00047
    • Peptide Name

    • Streptin 1 (Bacteriocin)
    • Source

    • Bacillus subtilis A1/3 (Gram-positive bacteria)
    • Family

    • Belongs to the type A lantibiotic family (Class I bacteriocin)
    • Gene

    • Not found
    • Sequence

    • VGSRYLCTPGSCWKLVCFTTTVK
    • Sequence Length

    • 23
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

    • Antimicrobial, Antibacterial
    • 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

    • Rich
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00047 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00047.
    • Formula

    • C114H181N29O31S3
    • Absent Amino Acids

    • ADEHIMNQ
    • Common Amino Acids

    • T
    • Mass

    • 2550.05
    • PI

    • 9.11
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +3
    • Boman Index

    • -10.25
    • Hydrophobicity

    • 0.4
    • Aliphatic Index

    • 71.74
    • Half Life

      • Mammalian:100 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 7115
    • Absorbance 280nm

    • 323.41
    • Polar Residues

    • 12

DRAMP00047

DRAMP00047 chydropathy plot
    • Two possible structures have been proposed for streptin 1 due to insufficient info. The first lanthionine S3-C7 and the second methyllanthionine T8-C12 are identical in the two proposed structures. A third intra-bond is either S11-C17 or C17-T19 (or C17-T20 or C17-T21). Compared to Streptin 1, Streptin 2 contains 3 additional residues TPY at the N-terminus. Small quantities of peptides at various degrees of dehydration were also detected.

  • ·Literature 1
    • Title

    • Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes.
    • Reference

    • Appl Environ Microbiol. 2003 May;69(5):2737-2747.
    • Author

    • Wescombe PA, Tagg JR.