Bacteriocin: Microcin J25

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Bacteriocin: Microcin J25

Accession: BAC015

Classification
Class: Unclassified
Genetics
Gene: mcjA
Producer and target organisms

Producer Organism: Escherichia coli [Gram-negative]

Taxonomy: BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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.
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).
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).
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).
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).
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).
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).
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).
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).
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End Note
Reference Manager
BibTeX
Gene structure
genome of Microcin J25

Gene idNameDescriptionLocation
BACGene18mcjAmicrocin J25 precursorcomplement(62..238)
BACGene19mcjBMcjB maturation of microcin J25578..1204
BACGene20mcjCMcjC maturation of microcin J251207..2535
BACGene21mcjDMcjD confers immunity ABC transporter homolog.2754..4496
mcjAmcjBmcjCmcjD
Protein sequence
 ........10 ........20 ........30 
          |          |          | 
 GGAGHVPEYF VGIGTPISFY G

Wheel representation
wheel representation of Microcin J25
3D Structure
Protein sequence annotations
Features of Microcin J25


FeaturePosition(s)LengthDescription
PEPTIDE1↔2121
Microcin J25.
Feature identifier = PRO_0000002775.
Cross-link1↔88Isoglutamyl glycine isopeptide (Gly-Glu).
STRAND5↔73
STRAND11↔144
STRAND18↔203
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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