ID   BCP_SHIFL               Reviewed;         156 AA.
AC   P0AE55; P23480;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=SF2523, S2673;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44026.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17839.1; -; Genomic_DNA.
DR   RefSeq; NP_708319.1; -.
DR   RefSeq; NP_838029.1; -.
DR   GeneID; 1024383; -.
DR   GeneID; 1078944; -.
DR   GenomeReviews; AE005674_GR; SF2523.
DR   GenomeReviews; AE014073_GR; S2673.
DR   KEGG; sfl:SF2523; -.
DR   KEGG; sfx:S2673; -.
DR   HOGENOM; P0AE55; -.
DR   OMA; P0AE55; LRDNMDD.
DR   BioCyc; SFLE198214:AAN44026.1-MON; -.
DR   BRENDA; 1.11.1.15; 189495.
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_0000135140.
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
//