General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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

    • Predicted Structure

    • There is no predicted structure for DRAMP00191.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.