ID   AHPC_STAA3              Reviewed;         189 AA.
AC   Q2FJN4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Alkyl hydroperoxide reductase C;
DE            EC=1.11.1.26 {ECO:0000250|UniProtKB:P0A251};
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=ahpC; OrderedLocusNames=SAUSA300_0380;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000250|UniProtKB:P0A251}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000250|UniProtKB:P0A251};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC       assemble to form a ring-like decamer. {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this typical 2-Cys
CC       peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide. The disulfide is subsequently reduced by AhpF.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000255; ABD22688.1; -; Genomic_DNA.
DR   RefSeq; WP_000052781.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FJN4; -.
DR   SMR; Q2FJN4; -.
DR   EnsemblBacteria; ABD22688; ABD22688; SAUSA300_0380.
DR   KEGG; saa:SAUSA300_0380; -.
DR   HOGENOM; CLU_042529_21_3_9; -.
DR   OMA; FWYPKDF; -.
DR   Proteomes; UP000001939; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102039; F:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR017559; AhpC.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..189
FT                   /note="Alkyl hydroperoxide reductase C"
FT                   /id="PRO_0000279760"
FT   DOMAIN          2..159
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        49
FT                   /note="Interchain (with C-168); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
FT   DISULFID        168
FT                   /note="Interchain (with C-49); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P0A251"
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