ID   AHPC_STAAW              Reviewed;         189 AA.
AC   P0A0B6; 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=MW0357;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB94222.1; -; Genomic_DNA.
DR   RefSeq; NP_645174.1; -.
DR   HSSP; P19479; 1N8J.
DR   PeroxiBase; 4924; SaurAhpC.
DR   GeneID; 1002457; -.
DR   GenomeReviews; BA000033_GR; MW0357.
DR   KEGG; sam:MW0357; -.
DR   HOGENOM; P0A0B6; -.
DR   OMA; P0A0B6; GDLADHY.
DR   BioCyc; SAUR196620:MW0357-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   3: Inferred from homology;
KW   Antioxidant; Complete proteome; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Redox-active center.
FT   CHAIN         1    189       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135127.
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
//