ID   BCP_HELPJ               Reviewed;         152 AA.
AC   Q9ZMU4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Putative peroxiredoxin bcp;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P0AE52};
DE   AltName: Full=Bacterioferritin comigratory protein homolog;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000305};
GN   Name=bcp; OrderedLocusNames=jhp_0124;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000250|UniProtKB:P0AE52}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P0AE52};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AE52}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC       peroxiredoxin, C(R) is present in the same subunit to form an
CC       intramolecular disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000250|UniProtKB:Q8P9V9}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE001439; AAD05701.1; -; Genomic_DNA.
DR   PIR; F71971; F71971.
DR   RefSeq; WP_000412964.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMU4; -.
DR   SMR; Q9ZMU4; -.
DR   STRING; 85963.jhp_0124; -.
DR   EnsemblBacteria; AAD05701; AAD05701; jhp_0124.
DR   GeneID; 66521388; -.
DR   KEGG; hpj:jhp_0124; -.
DR   PATRIC; fig|85963.30.peg.901; -.
DR   eggNOG; COG1225; Bacteria.
DR   OMA; RVVVYFY; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..152
FT                   /note="Putative peroxiredoxin bcp"
FT                   /id="PRO_0000135139"
FT   DOMAIN          4..152
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8P9V9"
FT   DISULFID        46..85
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q8P9V9"
SQ   SEQUENCE   152 AA;  17146 MW;  46DFE89F70D05DA1 CRC64;
     MEKLEVGQLA PDFRLKNSDG VEISLKDLLH KKVVLYFYPK DNTPGCTLEA KDFSALFSEF
     EKKNAVVVGV SPDNSQSHQK FISQCSLNVI LLCDEDKKVA NLYKAYGKRM LYGKEHLGII
     RSTFIINTQG VLEKCFYNVK AKGHAQKVLE SL