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Protein

Peroxiredoxin Bcp

Gene

bcp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.1 Publication

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Kineticsi

  1. KM=76.1 µM for H2O2 (using glutathione Grx1 as electron donor)1 Publication
  2. KM=99.5 µM for cumene hydroperoxide (using glutathione Grx1 as electron donor)1 Publication
  3. KM=6800 µM for tert-butyl hydroperoxide (using glutathione Grx1 as electron donor)1 Publication
  4. KM=14.6 µM for H2O2 (using thioredoxin Trx1 as electron donor)1 Publication
  5. KM=21.6 µM for cumene hydroperoxide (using thioredoxin Trx1 as electron donor)1 Publication
  6. KM=574 µM for tert-butyl hydroperoxide (using thioredoxin Trx1 as electron donor)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei46Cysteine sulfenic acid (-SOH) intermediate2 Publications1

    GO - Molecular functioni

    • hydroperoxide reductase activity Source: EcoCyc
    • thioredoxin peroxidase activity Source: EcoCyc

    GO - Biological processi

    • cell redox homeostasis Source: InterPro
    • response to oxidative stress Source: EcoCyc

    Keywordsi

    Molecular functionAntioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10108-MONOMER.
    MetaCyc:EG10108-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin Bcp (EC:1.11.1.15)
    Alternative name(s):
    Bacterioferritin comigratory protein
    Thioredoxin peroxidase
    Gene namesi
    Name:bcp
    Ordered Locus Names:b2480, JW2465
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10108. bcp.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001351341 – 156Peroxiredoxin BcpAdd BLAST156

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi46 ↔ 51Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP0AE52.
    PRIDEiP0AE52.

    2D gel databases

    SWISS-2DPAGEiP0AE52.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4260768. 12 interactors.
    851288. 1 interactor.
    IntActiP0AE52. 7 interactors.
    STRINGi316385.ECDH10B_2646.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AE52.
    SMRiP0AE52.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 156ThioredoxinPROSITE-ProRule annotationAdd BLAST153

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiENOG4108YXY. Bacteria.
    COG1225. LUCA.
    HOGENOMiHOG000022344.
    InParanoidiP0AE52.
    KOiK03564.
    PhylomeDBiP0AE52.

    Family and domain databases

    InterProiView protein in InterPro
    IPR000866. AhpC/TSA.
    IPR024706. Peroxiredoxin_AhpC-typ.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    PfamiView protein in Pfam
    PF00578. AhpC-TSA. 1 hit.
    PIRSFiPIRSF000239. AHPC. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiView protein in PROSITE
    PS51352. THIOREDOXIN_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AE52-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNPLKAGDIA PKFSLPDQDG EQVNLTDFQG QRVLVYFYPK AMTPGCTVQA
    60 70 80 90 100
    CGLRDNMDEL KKAGVDVLGI STDKPEKLSR FAEKELLNFT LLSDEDHQVC
    110 120 130 140 150
    EQFGVWGEKS FMGKTYDGIH RISFLIDADG KIEHVFDDFK TSNHHDVVLN

    WLKEHA
    Length:156
    Mass (Da):17,634
    Last modified:December 6, 2005 - v1
    Checksum:iC7D267A671409EFC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M63654 Genomic DNA. Translation: AAB88562.1.
    U00096 Genomic DNA. Translation: AAC75533.1.
    AP009048 Genomic DNA. Translation: BAA16358.1.
    AF023337 Genomic DNA. Translation: AAC46233.1.
    PIRiB49749.
    RefSeqiNP_416975.1. NC_000913.3.
    WP_001068682.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75533; AAC75533; b2480.
    BAA16358; BAA16358; BAA16358.
    GeneIDi946949.
    KEGGiecj:JW2465.
    eco:b2480.
    PATRICifig|1411691.4.peg.4259.

    Similar proteinsi

    Entry informationi

    Entry nameiBCP_ECOLI
    AccessioniPrimary (citable) accession number: P0AE52
    Secondary accession number(s): P23480
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: August 30, 2017
    This is version 90 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families