Bacteriocin: Microcin J25
Accession: BAC015
Classification
Class: Unclassified
Genetics
Gene: mcjA
Producer and target organisms
Producer Organism: Escherichia coli [Gram-negative]
Taxonomy: Bacteria
ProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organismsExhibits potent bacteriocidal activity against a range of Enterobacteriaceae -
including several pathogenic Escherichia coli - Salmonella - Shigella
Description
Mode of action:
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. 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. NOTE=Ref.2. NOTE=Ref.8. cyclic structure, but actually has a threaded side chain-to- backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif.
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. 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. NOTE=Ref.2. NOTE=Ref.8. cyclic structure, but actually has a threaded side chain-to- backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif.
Uniprot and PDB links
UniProt Entry: Q9X2V7
PDB Entry1PP5 resolved by NMR 1Q71 resolved by NMR 1S7P resolved by NMR
NUCLEOTIDE SEQUENCE [GENOMIC D+D301NA], STRAIN=AY25
MEDLINE=99214124;PubMed=10198038;
Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F., Salomon R.A.
"Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25.", J. Bacteriol. 181:2659-2662(1999).
MEDLINE=99214124;PubMed=10198038;
Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F., Salomon R.A.
"Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25.", J. Bacteriol. 181:2659-2662(1999).
PROTEIN SEQUENCE OF 38-58, AND MASS SPECTROMETRY.
PubMed=10092860;
Blond A., Peduzzi J., Goulard C., Chiuchiolo M.J., Barthelemy M., Prigent Y., Salomon R.A., Farias R.N., Moreno F., Rebuffat S.
"The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli.", Eur. J. Biochem. 259:747-755(1999).
PubMed=10092860;
Blond A., Peduzzi J., Goulard C., Chiuchiolo M.J., Barthelemy M., Prigent Y., Salomon R.A., Farias R.N., Moreno F., Rebuffat S.
"The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli.", Eur. J. Biochem. 259:747-755(1999).
CHARACTERIZATION.
PubMed=1429464;
Salomon R.A., Farias R.N.
"Microcin 25, a novel antimicrobial peptide produced by Escherichia coli.", J. Bacteriol. 174:7428-7435(1992).
PubMed=1429464;
Salomon R.A., Farias R.N.
"Microcin 25, a novel antimicrobial peptide produced by Escherichia coli.", J. Bacteriol. 174:7428-7435(1992).
FUNCTION.
PubMed=11731133;
Rintoul M.R., de Arcuri B.F., Salomon R.A., Farias R.N., Morero R.D.
"The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport.", FEMS Microbiol. Lett. 204:265-270(2001).
PubMed=11731133;
Rintoul M.R., de Arcuri B.F., Salomon R.A., Farias R.N., Morero R.D.
"The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport.", FEMS Microbiol. Lett. 204:265-270(2001).
FUNCTION.
PubMed=11443089;DOI=10.1128/JB.183.15.4543-4550.2001
Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A.
"Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.", J. Bacteriol. 183:4543-4550(2001).
PubMed=11443089;DOI=10.1128/JB.183.15.4543-4550.2001
Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A.
"Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.", J. Bacteriol. 183:4543-4550(2001).
FUNCTION.
PubMed=12401787;DOI=10.1074/jbc.M209425200
Yuzenkova J., Delgado M.A., Nechaev S., Savalia D., Epshtein V., Artsimovitch I., Mooney R.A., Landick R., Farias R.N., Salomon R.A., Severinov K.
"Mutations of bacterial RNA polymerase leading to resistance to microcin J25.", J. Biol. Chem. 277:50867-50875(2002).
PubMed=12401787;DOI=10.1074/jbc.M209425200
Yuzenkova J., Delgado M.A., Nechaev S., Savalia D., Epshtein V., Artsimovitch I., Mooney R.A., Landick R., Farias R.N., Salomon R.A., Severinov K.
"Mutations of bacterial RNA polymerase leading to resistance to microcin J25.", J. Biol. Chem. 277:50867-50875(2002).
MASS SPECTROMETRY, AND STRUCTURE BY NMR OF 38-58.
PubMed=14531661;DOI=10.1021/ja036677e
Bayro M.J., Mukhopadhyay J., Swapna G.V.T., Huang J.Y., Ma L.-C., Sineva E., Dawson P.E., Montelione G.T., Ebright R.H.
"Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.", J. Am. Chem. Soc. 125:12382-12383(2003).
PubMed=14531661;DOI=10.1021/ja036677e
Bayro M.J., Mukhopadhyay J., Swapna G.V.T., Huang J.Y., Ma L.-C., Sineva E., Dawson P.E., Montelione G.T., Ebright R.H.
"Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.", J. Am. Chem. Soc. 125:12382-12383(2003).
CHARACTERIZATION, MASS SPECTROMETRY, AND STRUCTURE BY NMR OF 38-58.
PubMed=14531690;DOI=10.1021/ja0367703
Rosengren K.J., Clark R.J., Daly N.L., Goeransson U., Jones A., Craik D.J.
"Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone.", J. Am. Chem. Soc. 125:12464-12474(2003).
PubMed=14531690;DOI=10.1021/ja0367703
Rosengren K.J., Clark R.J., Daly N.L., Goeransson U., Jones A., Craik D.J.
"Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone.", J. Am. Chem. Soc. 125:12464-12474(2003).
MASS SPECTROMETRY, AND STRUCTURE BY NMR OF 38-58.
PubMed=14531691;DOI=10.1021/ja036756q
Wilson K.-A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A.
"Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.", J. Am. Chem. Soc. 125:12475-12483(2003).
PubMed=14531691;DOI=10.1021/ja036756q
Wilson K.-A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A.
"Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.", J. Am. Chem. Soc. 125:12475-12483(2003).
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Gene structure
| Gene id | Name | Description | Location |
| BACGene18 | mcjA | microcin J25 precursor | complement(62..238) |
| BACGene19 | mcjB | McjB maturation of microcin J25 | 578..1204 |
| BACGene20 | mcjC | McjC maturation of microcin J25 | 1207..2535 |
| BACGene21 | mcjD | McjD confers immunity ABC transporter homolog. | 2754..4496 |
Protein sequence
| ........10 ........20 ........30 | | | GGAGHVPEYF VGIGTPISFY G |
Wheel representation
3D Structure
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔21 | 21 | Microcin J25. Feature identifier = PRO_0000002775.
|
| Cross-link | 1↔8 | 8 | Isoglutamyl glycine isopeptide (Gly-Glu). |
| STRAND | 5↔7 | 3 | |
| STRAND | 11↔14 | 4 | |
| STRAND | 18↔20 | 3 |
Composition
Hydrophobicity
Composition
| Formula | C101
H141
N23
O28
|
| Absent amino acids | CDKLMNQRW |
| Common amino acids | G |
| Mass (Da) | 2143.7 |
| Net charge | 0 |
| Isoelectric point | 5.36 |
| Basic residues | 1 |
| Acidic residues | 1 |
| Hydrophobic residues | 7 |
| Polar residues | 10 |
| Aliphatic residues | 4 |
| Tiny residues | 8 |
| Boman Index | 13.61 |
| Hydropathy Index | 0.4 |
| Aliphatic Index | 69.52 |
| Instability Index | 28.16 (stable) |
| Half Life |
Mammalian : 30 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 2980 M-1 cm-1 |
| Absorbance 280nm | 149 |
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