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   25-NOV-2008, entry version 47.
DE   RecName: Full=Putative peroxiredoxin bcp;
DE            EC=1.11.1.15;
DE   AltName: Full=Thioredoxin reductase;
DE   AltName: Full=Bacterioferritin comigratory protein homolog;
GN   Name=bcp; OrderedLocusNames=HP_0136;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; 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.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   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   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000511; AAD07205.1; -; Genomic_DNA.
DR   PIR; H64536; H64536.
DR   RefSeq; NP_206936.1; -.
DR   HSSP; Q63716; 1QQ2.
DR   DIP; DIP:3201N; -.
DR   GeneID; 900152; -.
DR   GenomeReviews; AE000511_GR; HP_0136.
DR   KEGG; hpy:HP0136; -.
DR   NMPDR; fig|85962.1.peg.134; -.
DR   TIGR; HP_0136; -.
DR   HOGENOM; P55979; -.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; AhpC-TSA.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN         1    152       Putative peroxiredoxin bcp.
FT                                /FTId=PRO_0000135138.
FT   DOMAIN        4    152       Thioredoxin.
FT   ACT_SITE     46     46       By similarity.
SQ   SEQUENCE   152 AA;  17116 MW;  40D71F05CC19D671 CRC64;
     MEKLEVGQLA PDFRLKNSDG VEISLKDLLH KKVVLYFYPK DNTPGCTLEA KDFSALFSEF
     EKKNAVVVGI SPDNAQSHQK FISQCSLNVI LLCDEDKKAA NLYKAYGKRM LYGKEHLGII
     RSTFIINTQG VLEKCFYNVK AKGHAQKVLE SL
//