• DRAMP ID

    • DRAMP00192
    • Peptide Name

    • Microcin C7 (MccC7; Microcin C51, MccC51; Bacteriocin)
    • Source

    • Escherichia coli (Gram-negative bacteria)
    • Family

    • Belongs to the class I microcin
    • Gene

    • mccA
    • Sequence

    • MRTGNAN
    • Sequence Length

    • 7
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, strains of Escherichia coli.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • It targets the aspartyl-tRNA synthetase
    • 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

    • Beta strand
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00192 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP00192.
    • Formula

    • C28H50N12O11S
    • Absent Amino Acids

    • CDEFHIKLPQSVWY
    • Common Amino Acids

    • N
    • Mass

    • 762.84
    • PI

    • 9.5
    • Basic Residues

    • 1
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 1
    • Net Charge

    • +1
    • Boman Index

    • -25.67
    • Hydrophobicity

    • -1.271
    • Aliphatic Index

    • 14.29
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP00192

    • Function

    • Inhibits protein translation by blocking aspartyl-tRNA synthetase Function
  • ·Literature 1
    • Title

    • Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.
    • Reference

    • J Mol Microbiol Biotechnol. 2007;13(4):200-209.
    • Author

    • Duquesne S, Petit V, Peduzzi J, Rebuffat S.
  • ·Literature 2
    • Title

    • Low-molecular-weight post-translationally modified microcins.
    • Reference

    • Mol Microbiol. 2007 Sep;65(6):1380-1394.
    • Author

    • Severinov K, Semenova E, Kazakov A, Kazakov T, Gelfand MS.
  • ·Literature 3
    • Title

    • How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.
    • Reference

    • EMBO J. 2009 Jul 8;28(13):1953-1964.
    • Author

    • Regni CA, Roush RF, Miller DJ, Nourse A, Walsh CT, Schulman BA.