View bacteriocin : Microcin J25

 Bookmark and Share

Accession BAC015
Name Microcin J25
Related Entries microcin B17 (MccB17)Microcin H47Microcin E492Colicin-V (Microcin-V)Microcin-24

Microcin C7
Gene mcjA
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae -

including several pathogenic Escherichia coli - Salmonella - Shigella
Swiss-Prot Entry Q9X2V7
PDB Entry 1PP5 resolved by NMR 1Q71 resolved by NMR 1S7P resolved by NMR
Other databases EMBL AF061787LinkHub Q9X2V7
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.
[Ref. 1] | View abstract | Export citation
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).

[Ref. 2] | View abstract | Export citation
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).

[Ref. 3] | View abstract | Export citation
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).

[Ref. 4] | View abstract | Export citation
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).

[Ref. 5] | View abstract | Export citation
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).

[Ref. 6] | View abstract | Export citation
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).

[Ref. 7] | View abstract | Export citation
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).

[Ref. 8] | View abstract | Export citation
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).

[Ref. 9] | View abstract | Export citation
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).

Loading...
End Note
Reference Manager
BibTeX
Sequence
 ........10 ........20 ........30 
          |          |          | 
 GGAGHVPEYF VGIGTPISFY G
Wheel representation
Structure
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
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Users comments for Microcin J25

No comments found

Login or register to submit a comment for Microcin J25.