• DRAMP ID

    • DRAMP00062
    • Peptide Name

    • Mersacidin (Bacteriocin; Preclinical)
    • Source

    • Bacillus sp. HIL-Y85/54728 (Gram-positive bacteria)
    • Family

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

    • mrsA
    • Sequence

    • CTFTLPGGGGVCTLTSECIC
    • Sequence Length

    • 20
    • Evidence code

    • Protein level
    • Biological Activity

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

      • Gram-positive bacteria: Methicillin-resistant Staphylococcus aureus, Vancomycin-resistant Enterococcus, Clostridium difficile.
    • Hemolytic Activity

      • N/A
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • The sugar phosphate head group of the peptidoglycan precursorLipid II
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Other Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Non helix or strand structure (Turn)
    • Structure Description

    • N/A
    • PDB ID

    • 1QOW resolved by NMR.
    • DRAMP00062 helical wheel diagram
    • Formula

    • C81H132N20O28S4
    • Absent Amino Acids

    • ADHKMNQRWY
    • Common Amino Acids

    • CGT
    • Mass

    • 2301.39
    • PI

    • 3.85
    • Basic Residues

    • 0
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 5
    • Boman Index

    • 10.17
    • Hydrophobicity

    • 94
    • Aliphatic Index

    • 73
    • Half Life

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

    • 250
    • Absorbance 280nm

    • 13.16
    • Polar Residues

    • 13

DRAMP00062

DRAMP00062 chydropathy plot
    • Function

    • Kills a number of Gram-positive bacteria. Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. May interact with the peptidoglycan precursor rather than with the enzyme.
    • PTM

    • There are one dihydroalanine (Dha)
  • Literature 1
    • Title

    • Cloning, sequencing and production of the lantibiotic mersacidin.
    • Reference

    • FEMS Microbiol Lett. 1995 Mar 15;127(1-2):121-126.
    • Author

    • Bierbaum G, Brötz H, Koller KP, Sahl HG.
  • Literature 2
    • Title

    • Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.
    • Reference

    • Eur J Biochem. 1997 Mar 1;244(2):501-512.
    • Author

    • Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler H, Griesinger C.
  • Literature 3
    • Title

    • Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster.
    • Reference

    • Appl Environ Microbiol. 2000 Jun;66(6):2565-2571.
    • Author

    • Altena K, Guder A, Cramer C, Bierbaum G.
  • Literature 4
    • Title

    • Ab initio structure determination of the lantibiotic mersacidin.
    • Reference

    • Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):705-713.
    • Author

    • Schneider TR, Kärcher J, Pohl E, Lubini P, Sheldrick GM.