ID   BCP_HELPY               Reviewed;         152 AA.
AC   P55979;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=HP_0136;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07205.1; -; Genomic_DNA.
DR   PIR; H64536; H64536.
DR   RefSeq; NP_206936.1; NC_000915.1.
DR   RefSeq; WP_000412947.1; NC_018939.1.
DR   AlphaFoldDB; P55979; -.
DR   SMR; P55979; -.
DR   DIP; DIP-3201N; -.
DR   IntAct; P55979; 21.
DR   MINT; P55979; -.
DR   STRING; 85962.C694_00670; -.
DR   PaxDb; P55979; -.
DR   PRIDE; P55979; -.
DR   EnsemblBacteria; AAD07205; AAD07205; HP_0136.
DR   KEGG; hpy:HP_0136; -.
DR   PATRIC; fig|85962.47.peg.147; -.
DR   eggNOG; COG1225; Bacteria.
DR   OMA; RVVVYFY; -.
DR   PhylomeDB; P55979; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..152
FT                   /note="Putative peroxiredoxin bcp"
FT                   /id="PRO_0000135138"
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;  17116 MW;  40D71F05CC19D671 CRC64;
     MEKLEVGQLA PDFRLKNSDG VEISLKDLLH KKVVLYFYPK DNTPGCTLEA KDFSALFSEF
     EKKNAVVVGI SPDNAQSHQK FISQCSLNVI LLCDEDKKAA NLYKAYGKRM LYGKEHLGII
     RSTFIINTQG VLEKCFYNVK AKGHAQKVLE SL