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Q9X2V7

- MCJA_ECOLX

UniProt

Q9X2V7 - MCJA_ECOLX

Protein

Microcin J25

Gene

mcjA

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 446
    Beta strandi48 – 514
    Beta strandi55 – 573

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PP5NMR-A38-58[»]
    1Q71NMR-A38-58[»]
    1S7PNMR-A38-47[»]
    B48-58[»]
    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

    MIKHFHFNKL SSGKKNNVPS PAKGVIQIKK SASQLTKGGA GHVPEYFVGI   50
    GTPISFYG 58
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061787 Genomic DNA. Translation: AAD28494.1.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Entanglement - Issue 72 of July 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061787 Genomic DNA. Translation: AAD28494.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PP5 NMR - A 38-58 [» ]
    1Q71 NMR - A 38-58 [» ]
    1S7P NMR - A 38-47 [» ]
    B 48-58 [» ]
    2MMW NMR - A 38-58 [» ]
    4CU4 X-ray 2.30 B 38-58 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60856N.

    Protein family/group databases

    TCDBi 9.A.52.1.1. the microcin j25 (microsin j25) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9X2V7.

    Family and domain databases

    ProtoNeti Search...

    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: October 1, 2014
    This is version 56 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