ID   AHPC_STAAM              Reviewed;         189 AA.
AC   P0A0B5; Q53647;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit C;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=ahpC; OrderedLocusNames=SAV0381;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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-49-SH group is the primary site of oxidation by
CC       H(2)O(2), and the oxidized Cys-49 (probably Cys-SOH) rapidly
CC       reacts with Cys-168-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; BA000017; BAB56543.1; -; Genomic_DNA.
DR   RefSeq; NP_370905.1; -.
DR   HSSP; P19479; 1N8J.
DR   World-2DPAGE; 0002:P0A0B5; -.
DR   GeneID; 1120338; -.
DR   GenomeReviews; BA000017_GR; SAV0381.
DR   KEGG; sav:SAV0381; -.
DR   HOGENOM; P0A0B5; -.
DR   OMA; P0A0B5; GDLADHY.
DR   BioCyc; SAUR158878:SAV0381-MON; -.
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; 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   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Complete proteome; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Redox-active center.
FT   CHAIN         1    189       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135123.
FT   DOMAIN        2    159       Thioredoxin.
FT   ACT_SITE     49     49       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID     49     49       Interchain (with C-168); in linked form
FT                                (By similarity).
FT   DISULFID    168    168       Interchain (with C-49); in linked form
FT                                (By similarity).
SQ   SEQUENCE   189 AA;  20977 MW;  B7134A9C84066B73 CRC64;
     MSLINKEILP FTAQAFDPKK DQFKEVTQED LKGSWSVVCF YPADFSFVCP TELEDLQNQY
     EELQKLGVNV FSVSTDTHFV HKAWHDHSDA ISKITYTMIG DPSQTITRNF DVLDEATGLA
     QRGTFIIDPD GVVQASEINA DGIGRDASTL AHKIKAAQYV RKNPGEVCPA KWEEGAKTLQ
     PGLDLVGKI
//