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Protein

Microcin J25

Gene

mcjA

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin

Protein family/group databases

TCDBi9.A.52.1.1. the microcin j25 (microsin j25) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Microcin J25
Short name:
MccJ25
Gene namesi
Name:mcjA
Encoded oniPlasmid pTUC1000 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 37371 PublicationPRO_0000002774Add
BLAST
Peptidei38 – 5821Microcin J25PRO_0000002775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki38 ↔ 45Isoglutamyl glycine isopeptide (Gly-Glu)

Keywords - PTMi

Isopeptide bond

Expressioni

Inductioni

At the onset of stationary growth phase.

Interactioni

Protein-protein interaction databases

DIPiDIP-60856N.

Structurei

Secondary structure

1
58
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi48 – 514Combined sources
Beta strandi55 – 573Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PP5NMR-A38-58[»]
1Q71NMR-A38-58[»]
1S7PNMR-A38-47[»]
B48-58[»]
2MMTNMR-A38-58[»]
2MMWNMR-A38-58[»]
4CU4X-ray2.30B38-58[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2V7.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9X2V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKHFHFNKL SSGKKNNVPS PAKGVIQIKK SASQLTKGGA GHVPEYFVGI

GTPISFYG
Length:58
Mass (Da):6,200
Last modified:November 1, 1999 - v1
Checksum:iA9F4393C8EAAC8FA
GO

Mass spectrometryi

Molecular mass is 2107.0 Da from positions 38 - 58. Determined by ESI. 1 Publication
Molecular mass is 2106.0 Da from positions 38 - 58. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061787 Genomic DNA. Translation: AAD28494.1.
RefSeqiWP_001513516.1. NZ_JSRQ01000010.1.
YP_009071192.1. NC_025179.1.
YP_009075876.1. NG_035155.1.

Genome annotation databases

GeneIDi20493264.

Cross-referencesi

Web resourcesi

Protein Spotlight

Entanglement - Issue 72 of July 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061787 Genomic DNA. Translation: AAD28494.1.
RefSeqiWP_001513516.1. NZ_JSRQ01000010.1.
YP_009071192.1. NC_025179.1.
YP_009075876.1. NG_035155.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PP5NMR-A38-58[»]
1Q71NMR-A38-58[»]
1S7PNMR-A38-47[»]
B48-58[»]
2MMTNMR-A38-58[»]
2MMWNMR-A38-58[»]
4CU4X-ray2.30B38-58[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60856N.

Protein family/group databases

TCDBi9.A.52.1.1. the microcin j25 (microsin j25) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20493264.

Miscellaneous databases

EvolutionaryTraceiQ9X2V7.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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. Cited for: FUNCTION.
  7. 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.

Entry informationi

Entry nameiMCJA_ECOLX
AccessioniPrimary (citable) accession number: Q9X2V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally 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.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.