Record in detail


General Info

  • lamp_id:L01A002803
  • Name:MCCC7_ECOLX
  • FullName:Microcin C7
  • Source:Escherichia coli
  • Mass:2145.6 Da
  • Sequence Length:7 aa
  • Isoelectric Point:10.55
  • Activity:Antibacterial
  • Sequence
        MRTGNAN
  • Function:Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.

Cross-Linking

Top similar AMPs

  • Top similar AMPs on LAMP

  •     No similar AMPs found on LAMP database

Structure

  •   Domains

  •     No domains found on LAMP database
  •   Structures
  •   1
    PDB:3H5R

    Method:X-ray
    Chains:E/F/G/H=1-7
  •   2
    PDB:3H9G

    Method:X-ray
    Chains:E/F/G/H=1-7
  •   3
    PDB:3H9J

    Method:X-ray
    Chains:E/F/G/H=1-7
  •   4
    PDB:3H9Q

    Method:X-ray
    Chains:E/F/G/H=1-7

Activity

  •   Antibacterial Activities

  •     No MICs found on LAMP database

Toxicity

  •   Toxicity

  •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Mendez E.,Pezzi N.,Garcia-Bustos J.F.,
  •   Title:Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.
  •   Journal:Antimicrob. Agents Chemother., 1985, 27, 791-797  [PubMed:2861788]
  •   [2]  Moreno F.,San Millan J.L.,Gonzalez-Pastor J.E.,
  •   Title:The smallest known gene.
  •   Journal:Nature, 1994, 369, 281-281  [MEDLINE:94239518]
  •   [3]  Castilla M.A.,San Millan J.L.,Baleux F.,Gonzalez-Pastor J.E.,Guijarro J.I.,
  •   Title:Chemical structure and translation inhibition studies of the antibiotic microcin C7.
  •   Journal:J. Biol. Chem., 1995, 270, 23520-23532  [PubMed:7559516]
  •   [4]  Moreno F.,Castilla M.A.,San Millan J.L.,Gonzalez-Pastor J.E.,
  •   Title:Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7.
  •   Journal:J. Bacteriol., 1995, 177, 7131-7140  [MEDLINE:96099297]
  •   [5]  Egorov T.A.,Zaitsev D.A.,Shashkov A.S.,Katrukha G.S.,Metlitskaya A.Z.,
  •   Title:Structure of microcin C51, a new antibiotic with a broad spectrum of activity.
  •   Journal:FEBS Lett., 1995, 357, 235-238  [PubMed:7835418]
  •   [6]  Praetorius-Ibba M.,Pavlova O.,Kommer A.,Kazakov T.,Metlitskaya A.Z.,
  •   Title:Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic microcin C.
  •   Journal:J. Biol. Chem., 2006, 281, 18033-18042  [PubMed:16574659]
  •   [7]  Gelfand M.S.,Kazakov T.,Kazakov A.,Semenova E.,Severinov K.,
  •   Title:Low-molecular-weight post-translationally modified microcins.
  •   Journal:Mol. Microbiol., 2007, 65, 1380-1394  [PubMed:17711420]
  •   [8]  Rebuffat S.,Peduzzi J.,Petit V.,Duquesne S.,
  •   Title:Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.
  •   Journal:J. Mol. Microbiol. Biotechnol., 2007, 13, 200-209  [PubMed:17827970]
  •   [9]  Metlitskaya A.Z.,Novikova M.,Datsenko K.A.,Vondenhoff G.H.,Kazakov T.,
  •   Title:Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.
  •   Journal:J. Bacteriol., 2008, 190, 2607-2610  [PubMed:18223070]

Comments

  •   Comments

  •     No comments found on LAMP database



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