ID   AHPC_SHIFL              Reviewed;         187 AA.
AC   P0AE11; P26427;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit C;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Alkyl hydroperoxide reductase protein C22;
DE   AltName: Full=SCRP-23;
DE   AltName: Full=Sulfate starvation-induced protein 8;
DE            Short=SSI8;
GN   Name=ahpC; OrderedLocusNames=SF0524, S0529;
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   -!- FUNCTION: Directly reduces organic hydroperoxides in its reduced
CC       dithiol form (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By
CC       similarity).
CC   -!- PTM: The Cys-47-SH group is the primary site of oxidation by
CC       H(2)O(2), and the oxidized Cys-47 (probably Cys-SOH) rapidly
CC       reacts with Cys-166-SH of the other subunit to form an
CC       intermolecular disulfide. This disulfide is subsequently reduced
CC       by thioredoxin (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AE005674; AAN42170.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16040.1; -; Genomic_DNA.
DR   RefSeq; NP_706463.1; -.
DR   RefSeq; NP_836234.1; -.
DR   HSSP; P19479; 1N8J.
DR   SMR; P0AE11; 2-187.
DR   GeneID; 1023440; -.
DR   GeneID; 1076966; -.
DR   GenomeReviews; AE005674_GR; SF0524.
DR   GenomeReviews; AE014073_GR; S0529.
DR   KEGG; sfl:SF0524; -.
DR   KEGG; sfx:S0529; -.
DR   HOGENOM; P0AE11; -.
DR   OMA; P0AE11; GDLADHY.
DR   BioCyc; SFLE198214:AAN42170.1-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; IPR017559; Peroxiredoxin.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Antioxidant; Complete proteome; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    187       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135121.
FT   DOMAIN        2    157       Thioredoxin.
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   MOD_RES      17     17       N6-acetyllysine (By similarity).
FT   MOD_RES      93     93       N6-acetyllysine (By similarity).
FT   MOD_RES     153    153       N6-acetyllysine (By similarity).
FT   MOD_RES     169    169       N6-acetyllysine (By similarity).
FT   MOD_RES     171    171       N6-acetyllysine (By similarity).
FT   DISULFID     47     47       Interchain (with C-166); in linked form
FT                                (By similarity).
FT   DISULFID    166    166       Interchain (with C-47); in linked form
FT                                (By similarity).
SQ   SEQUENCE   187 AA;  20761 MW;  40AB796E6F5CC2D6 CRC64;
     MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
     LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
     ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS
     LDLVGKI
//