ID   AHPC_SALTI              Reviewed;         187 AA.
AC   P0A252; P19479;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 31.
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;
GN   Name=ahpC; OrderedLocusNames=STY0653, t2260;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   MEDLINE=22531367; PubMed=12644504;
RX   DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Directly reduces alkyl hydroperoxides with the use of
CC       electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide
CC       reductase (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.
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; AL627267; CAD05084.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69862.1; -; Genomic_DNA.
DR   RefSeq; NP_455184.1; -.
DR   RefSeq; NP_806002.1; -.
DR   SMR; P0A252; 2-187.
DR   GeneID; 1069351; -.
DR   GeneID; 1247116; -.
DR   GenomeReviews; AE014613_GR; t2260.
DR   GenomeReviews; AL513382_GR; STY0653.
DR   KEGG; stt:t2260; -.
DR   KEGG; sty:STY0653; -.
DR   HOGENOM; P0A252; -.
DR   OMA; P0A252; GDLADHY.
DR   BioCyc; SENT209261:T2260-MON; -.
DR   BioCyc; SENT220341:STY0653-MON; -.
DR   BRENDA; 1.11.1.15; 3716.
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   Antioxidant; Complete proteome; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    187       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135119.
FT   DOMAIN        2    157       Thioredoxin.
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate (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;  20747 MW;  83B251C74DE9860D CRC64;
     MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
     LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
     ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAA HPGEVCPAKW KEGEATLAPS
     LDLVGKI
//