ID   BCP_ECOL6               Reviewed;         156 AA.
AC   P0AE53; P23480;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=c3008;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81458.1; -; Genomic_DNA.
DR   RefSeq; NP_754890.1; -.
DR   GeneID; 1038668; -.
DR   GenomeReviews; AE014075_GR; c3008.
DR   KEGG; ecc:c3008; -.
DR   HOGENOM; P0AE53; -.
DR   OMA; P0AE53; LRDNMDD.
DR   BRENDA; 1.11.1.15; 292881.
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; Alkyl_hydroperoxide_Rdtase.
DR   InterPro; IPR017936; Thioredoxin-like.
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_0000135136.
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
//