• DRAMP ID

    • DRAMP00191
    • Peptide Name

    • Microcin J25 (MccJ25; Bacteriocin)
    • Source

    • Escherichia coli AY25 (Gram-negative bacteria)
    • Family

    • Belongs to the class I microcin
    • Gene

    • mcjA
    • Sequence

    • GGAGHVPEYFVGIGTPISFYG
    • Sequence Length

    • 21
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli BM21 (MIC=0.08 µg/ml), E. coli AB1133 (MIC=0.02 µg/ml), E. coli RYC816 (MIC=0.04 µg/ml), E. coli AY29 (MIC=0.04 µg/ml), Salmonella species, Shigella flexneri.
    • Hemolytic Activity

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

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Cyclization of a N-terminal between Gly and Glu
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Beta strand
    • Structure Description

    • MccJ25 does not have a head-to-tail cyclic structure but rather a side chain to backbone cyclization between Glu8 and the N-terminus. This creates an embedded ring that is threaded by the C-terminal tail of the molecule, forming a noose-like feature. The three-dimensional structure deduced from NMR data suggests that slippage of the noose is prevented by two aromatic residues flanking the embedded ring.
    • Helical Wheel Diagram

    • DRAMP00191 helical wheel diagram
  • 1Q71-> 
    1PP5-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP00191.
    • Formula

    • C101H141N23O28
    • Absent Amino Acids

    • CDKLMNQRW
    • Common Amino Acids

    • G
    • Mass

    • 2125.37
    • PI

    • 5.24
    • Basic Residues

    • 1
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 7
    • Net Charge

    • 0
    • Boman Index

    • 13.61
    • Hydrophobicity

    • 0.4
    • Aliphatic Index

    • 69.52
    • Half Life

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

    • 2980
    • Absorbance 280nm

    • 149
    • Polar Residues

    • 10

DRAMP00191

DRAMP00191 chydropathy plot
    • Function

    • Microcin J25 is a 21 amino acid bacterial peptide that has potent antibacterial activity against Gram-negative bacteria, resulting from its interaction with RNA polymerase.
    • Induction

    • At the onset of stationary growth phase.
    • PTM

    • Isoglutamyl glycine isopeptide between G1 and E8.
  • ·Literature 1
    • Title

    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli.
    • Reference

    • J Bacteriol. 1992 Nov;174(22):7428-7435.
    • Author

    • Salom³n RA, Far­as RN.
  • ·Literature 2
    • Title

    • The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli.
    • Reference

    • Eur J Biochem. 1999 Feb;259(3):747-755.
    • Author

    • Blond A, P©duzzi J, Goulard C, Chiuchiolo MJ, Barth©l©my M, Prigent Y, Salom³n RA, Far­as RN, Moreno F, Rebuffat S.
  • ·Literature 3
    • Title

    • Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone.
    • Reference

    • J Am Chem Soc. 2003 Oct 15;125(41):12464-74.
    • Author

    • Rosengren KJ, Clark RJ, Daly NL, Göransson U, Jones A, Craik DJ.
  • ·Literature 4
    • Title

    • Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.
    • Reference

    • J Am Chem Soc. 2003 Oct 15;125(41):12382-3.
    • Author

    • Bayro MJ, Mukhopadhyay J, Swapna GV, Huang JY, Ma LC, Sineva E, Dawson PE, Montelione GT, Ebright RH.