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Q9X2V7 (MCJA_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microcin J25

Short name=MccJ25
Gene names
Name:mcjA
Encoded onPlasmid pTUC100
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length58 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5 Ref.6

Subcellular location

Secreted.

Induction

At the onset of stationary growth phase.

Caution

Was originally (Ref.2) thought to have a head-to-tail 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.

Mass spectrometry

Molecular mass is 2107.0 Da from positions 38 - 58. Determined by ESI. Ref.2

Molecular mass is 2106.0 Da from positions 38 - 58. Determined by MALDI. Ref.8

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAntibiotic
Antimicrobial
Bacteriocin
   PTMIsopeptide bond
   Technical term3D-structure
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 3737
PRO_0000002774
Peptide38 – 5821Microcin J25 Ref.2
PRO_0000002775

Amino acid modifications

Cross-link38 ↔ 45Isoglutamyl glycine isopeptide (Gly-Glu)

Secondary structure

....... 58
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X2V7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A9F4393C8EAAC8FA

FASTA586,200
        10         20         30         40         50 
MIKHFHFNKL SSGKKNNVPS PAKGVIQIKK SASQLTKGGA GHVPEYFVGI GTPISFYG 

« Hide

References

[1]"Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25."
Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F., Salomon R.A.
J. Bacteriol. 181:2659-2662(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AY25.
[2]"The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli."
Blond A., Peduzzi J., Goulard C., Chiuchiolo M.J., Barthelemy M., Prigent Y., Salomon R.A., Farias R.N., Moreno F., Rebuffat S.
Eur. J. Biochem. 259:747-755(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-58, MASS SPECTROMETRY.
[3]"Microcin 25, a novel antimicrobial peptide produced by Escherichia coli."
Salomon R.A., Farias R.N.
J. Bacteriol. 174:7428-7435(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport."
Rintoul M.R., de Arcuri B.F., Salomon R.A., Farias R.N., Morero R.D.
FEMS Microbiol. Lett. 204:265-270(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25."
Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A.
J. Bacteriol. 183:4543-4550(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Mutations of bacterial RNA polymerase leading to resistance to microcin J25."
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.
J. Biol. Chem. 277:50867-50875(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot."
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.
J. Am. Chem. Soc. 125:12382-12383(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 38-58, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone."
Rosengren K.J., Clark R.J., Daly N.L., Goeransson U., Jones A., Craik D.J.
J. Am. Chem. Soc. 125:12464-12474(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58.
[9]"Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail."
Wilson K.-A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A.
J. Am. Chem. Soc. 125:12475-12483(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 38-58, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Entanglement - Issue 72 of July 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061787 Genomic DNA. Translation: AAD28494.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PP5NMR-A38-58[»]
1Q71NMR-A38-58[»]
1S7PNMR-A38-47[»]
B48-58[»]
2MMWNMR-A38-58[»]
4CU4X-ray2.30B38-58[»]
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB9.A.52.1.1. the microcin j25 (microsin j25) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceQ9X2V7.

Entry information

Entry nameMCJA_ECOLX
AccessionPrimary (citable) accession number: Q9X2V7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references