ID   AHPC_STAHJ              Reviewed;         189 AA.
AC   Q4L376;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=SH2592;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05901.1; -; Genomic_DNA.
DR   RefSeq; YP_254507.1; -.
DR   GeneID; 3482442; -.
DR   GenomeReviews; AP006716_GR; SH2592.
DR   KEGG; sha:SH2592; -.
DR   NMPDR; fig|279808.3.peg.1207; -.
DR   HOGENOM; Q4L376; -.
DR   OMA; Q4L376; GDLADHY.
DR   BioCyc; SHAE279808:SH2592-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_0000279761.
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;  21047 MW;  2A1F87D0EFB461AF CRC64;
     MSLINKEILP FIAQAYDPKK DEFKEVSQDD LKGSWSVVCF YPADFSFVCP TELEDLQNQY
     DKLQDLGVNV FSVSTDTHFV HKAWHDHSDA ISKIQYQMIG DPSQTITRNF DVLDEEAGLA
     QRGTFIIDPD GVVQAAEINA DGIGRDASTL VNKIKAAQYV RQHPGEVCPA KWEEGSESLQ
     PGLDLVGKI
//