• DRAMP ID

    • DRAMP00222
    • Peptide Name

    • Microcin E492 (MccE492; Bacteriocin)
    • Source

    • Klebsiella pneumoniae RYC492 (Gram-negative bacteria)
    • Family

    • Unknown
    • Gene

    • mceA
    • Sequence

    • GETDPNTQLLNDLGNNMAWGAALGAPGGLGSAALGAAGGALQTVGQGLIDHGPVNVFIPVLIGPSWNGSGSGYNSATSSSGSGS
    • Sequence Length

    • 84
    • Evidence code

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli F (MIC=0.14 µM), Escherichia coli 363 (MIC=0.02 µM), Escherichia coli ML35p (MIC=0.14 µM), Escherichia coli GM1 (MIC=0.04 µM), Escherichia coli GM1 KP1060(MIC=0.65 µM), Escherichia coli W3110 (MIC=0.02 µM), Escherichia coli W3110-KP1344 Pms7 (MIC=0.08 µM), Escherichia coli W3110-6 (MIC=0.32 µM), Escherichia coli C600 (MIC=0.08 µM), Escherichia coli C600 pHX405 (MIC=0.16 µM), Salmonella enteritidis (MIC=0.6 µM), Salmonella typhimurium (MIC=1.2 µM).
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP00222 helical wheel diagram
    • Formula

    • C342H532N98O118S
    • Absent Amino Acids

    • CKR
    • Common Amino Acids

    • G
    • Mass

    • 9417.32
    • PI

    • 3.7
    • Basic Residues

    • 1
    • Acidic Residues

    • 4
    • Hydrophobic Residues

    • 29
    • Boman Index

    • -24
    • Hydrophobicity

    • 6.55
    • Aliphatic Index

    • 81.43
    • Half Life

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

    • 12490
    • Absorbance 280nm

    • 150.48
    • Polar Residues

    • 41

DRAMP00222

DRAMP00222 chydropathy plot
    • Function

    • Channel-forming bacteriocin. Forms cation-selective channels. Active on enterobacteria, with highest activity against Escherichia coli. The unmodified protein is active against Escherichia coli and S. enteritidis. When the siderophore ester is present at Ser-99, antibacterial activity against these species is increased and activity is also detected against E. cloacae and K. pneumoniae.
    • PTM

    • The C-terminal Ser is modified by attachment to a siderophore similar to enterobactin, which can bind one atom of iron. The modification consists of an ester linkage of the serine carboxyl to O6 of a glucose which is linked by a C-glycosidic bond to the 5'-benzoyl of a linear triester of N-(2,3-dihydroxybenzoyl)serine. Presence of the siderophore ester increases the antibacterial activity of the protein.
  • Literature 1
    • Reference

    • Mol Microbiol. 2003 Aug;49(4):1031-1041.
    • Author

    • Destoumieux-Garz³n D, Thomas X, Santamaria M, Goulard C, Barth©l©my M, Boscher B, Bessin Y, Molle G, Pons AM, Letellier L, Peduzzi J, Rebuffat S.
    • Title

    • Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.
  • Literature 2
    • Reference

    • J Biol Chem. 2004 Jul 2;279(27):28233-28242.
    • Author

    • Thomas X, Destoumieux-Garz³n D, Peduzzi J, Afonso C, Blond A, Birlirakis N, Goulard C, Dubost L, Thai R, Tabet JC, Rebuffat S.
    • Title

    • Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.
  • Literature 3
    • Reference

    • FEBS Lett. 1993 Apr 26;321(2-3):145-148.
    • Author

    • Lagos R, Wilkens M, Vergara C, Cecchi X, Monasterio O.
    • Title

    • Microcin E492 forms ion channels in phospholipid bilayer membrane.