Record in detail


General Info

  • lamp_id:L01A003297
  • Name:MCJA_ECOLX
  • FullName:Microcin J25
  • Source:Escherichia coli
  • Mass:2125.4 Da
  • Sequence Length:21 aa
  • Isoelectric Point:5.37
  • Activity:Antibacterial
  • Sequence
        GGAGHVPEYFVGIGTPISFYG
  • Function:Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins.

Cross-Linking

Top similar AMPs

  • Top similar AMPs on LAMP
  • 1. L12A07544|    From 38 To 58 E-value: 0.0000003 Score: 45.4
        GGAGHVPEYFVGIGTPISFYG
  • 2. L01A003297    From 1 To 21 E-value: 0.000001 Score: 43.1
        GGAGHVPEYFVGIGTPISFYG
  • 3. L12A02716|    From 1 To 10 E-value: 0.76 Score: 24.3
        GGAGHVPEYF
  • 4. L13A011962    From 1 To 11 E-value: 0.83 Score: 23.9
        VGIGTPISFYG
  • 5. L13A011962    From 12 To 21 E-value: 0.88 Score: 23.9
        GGAGHVPEYF

Structure

  •   Domains

    •     No domains found on LAMP database
  •   Structures
  •   1
    PDB:1PP5
    Method:NMR
    Chains:A=38-58
  •   2
    PDB:1Q71
    Method:NMR
    Chains:A=38-58
  •   3
    PDB:1S7P
    Method:NMR
    Chains:A=38-47, B=48-58
  •   4
    PDB:1PP5
    Method:NMR
    Chains:A=38-58
  •   5
    PDB:1Q71
    Method:NMR
    Chains:A=38-58
  •   6
    PDB:1S7P
    Method:NMR
    Chains:A=38-47, B=48-58

Activity

  •   Antibacterial Activities
  •   1  Target:  E. coli BM21  MIC:  0.08 μg/ml  (0.03764 μM)  
  •   2  Target:  E. coli AB1133  MIC:  0.02 μg/ml  (0.00940999 μM)  
  •   3  Target:  E. coli RYC816  MIC:  0.04 μg/ml  (0.01882 μM)  
  •   4  Target:  E. coli AY29  MIC:  0.04 μg/ml  (0.01882 μM)  
  •   5  Target:  S. newport  MIC:  0.01 μg/ml  (0.004705 μM)  

Toxicity

  •   Toxicity

    •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Farias R.N.,Salomon R.A.,
  •   Title:Microcin 25, a novel antimicrobial peptide produced by Escherichia coli.
  •   Journal:J. Bacteriol., 1992, 174, 7428-7435  [PubMed:1429464]
  •   [2]  Moreno F.,Gonzalez-Pastor J.E.,Farias R.N.,Ciaccio M.,Solbiati J.O.,
  •   Title:Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25.
  •   Journal:J. Bacteriol., 1999, 181, 2659-2662  [MEDLINE:99214124]
  •   [3]  Barthelemy M.,Chiuchiolo M.J.,Goulard C.,Peduzzi J.,Blond A.,
  •   Title:The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli.
  •   Journal:Eur. J. Biochem., 1999, 259, 747-755  [PubMed:10092860]
  •   [4]  Salomon R.A.,Farias R.N.,Rintoul M.R.,Delgado M.A.,
  •   Title:Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.
  •   Journal:J. Bacteriol., 2001, 183, 4543-4550  [PubMed:11443089]
  •   [5]  Morero R.D.,Farias R.N.,Salomon R.A.,de Arcuri B.F.,Rintoul M.R.,
  •   Title:The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport.
  •   Journal:FEMS Microbiol. Lett., 2001, 204, 265-270  [PubMed:11731133]
  •   [6]  Epshtein V.,Savalia D.,Nechaev S.,Delgado M.A.,Yuzenkova J.,
  •   Title:Mutations of bacterial RNA polymerase leading to resistance to microcin J25.
  •   Journal:J. Biol. Chem., 2002, 277, 50867-50875  [PubMed:12401787]
  •   [7]  Jones A.,Goeransson U.,Daly N.L.,Clark R.J.,Rosengren K.J.,
  •   Title:Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone.
  •   Journal:J. Am. Chem. Soc., 2003, 125, 12464-12474  [PubMed:14531690]
  •   [8]  Ma L.-C.,Huang J.Y.,Swapna G.V.T.,Mukhopadhyay J.,Bayro M.J.,
  •   Title:Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.
  •   Journal:J. Am. Chem. Soc., 2003, 125, 12382-12383  [PubMed:14531661]
  •   [9]  Chait B.T.,Yuzenkova J.,Ottesen J.,Kalkum M.,Wilson K.-A.,
  •   Title:Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.
  •   Journal:J. Am. Chem. Soc., 2003, 125, 12475-12483  [PubMed:14531691]

Comments

  •   Comments

    •     No comments found on LAMP database



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