ID   BCP_ECO57               Reviewed;         156 AA.
AC   P0AE54; P23480;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   04-NOV-2008, entry version 21.
DE   RecName: Full=Putative peroxiredoxin bcp;
DE            EC=1.11.1.15;
DE   AltName: Full=Thioredoxin reductase;
DE   AltName: Full=Bacterioferritin comigratory protein;
GN   Name=bcp; OrderedLocusNames=Z3739, ECs3342;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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.
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DR   EMBL; AE005174; AAG57590.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36765.1; -; Genomic_DNA.
DR   PIR; B85891; B85891.
DR   PIR; F91046; F91046.
DR   RefSeq; NP_289033.1; -.
DR   RefSeq; NP_311369.1; -.
DR   GeneID; 915247; -.
DR   GeneID; 957792; -.
DR   GenomeReviews; BA000007_GR; ECs3342.
DR   GenomeReviews; AE005174_GR; Z3739.
DR   KEGG; ece:Z3739; -.
DR   KEGG; ecs:ECs3342; -.
DR   HOGENOM; P0AE54; -.
DR   BioCyc; ECOL83334:ECS3342-MON; -.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
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    156       Putative peroxiredoxin bcp.
FT                                /FTId=PRO_0000135135.
FT   DOMAIN        4    156       Thioredoxin.
FT   ACT_SITE     46     46       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
SQ   SEQUENCE   156 AA;  17634 MW;  C7D267A671409EFC CRC64;
     MNPLKAGDIA PKFSLPDQDG EQVNLTDFQG QRVLVYFYPK AMTPGCTVQA CGLRDNMDEL
     KKAGVDVLGI STDKPEKLSR FAEKELLNFT LLSDEDHQVC EQFGVWGEKS FMGKTYDGIH
     RISFLIDADG KIEHVFDDFK TSNHHDVVLN WLKEHA
//