ID   AHPC_STAA8              Reviewed;         189 AA.
AC   P0A0B7; Q2G0Z6; Q53647;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=SAOUHSC_00365;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, AND
RP   INDUCTION BY OSMOTIC UPSHOCK.
RX   MEDLINE=96004465; PubMed=7551034;
RA   Armstrong-Buisseret L., Cole M.B., Stewart G.S.A.B.;
RT   "A homologue to the Escherichia coli alkyl hydroperoxide reductase
RT   AhpC is induced by osmotic upshock in Staphylococcus aureus.";
RL   Microbiology 141:1655-1661(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC8325 genome.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION BY METALS, AND REGULATION BY FUR AND PERR.
RX   PubMed=14742543; DOI=10.1128/IAI.72.2.972-979.2004;
RA   Morrissey J.A., Cockayne A., Brummell K., Williams P.;
RT   "The staphylococcal ferritins are differentially regulated in response
RT   to iron and manganese and via perR and fur.";
RL   Infect. Immun. 72:972-979(2004).
RN   [4]
RP   FUNCTION, AND REGULATION BY PERR.
RX   PubMed=17114262; DOI=10.1128/JB.01524-06;
RA   Cosgrove K., Coutts G., Jonsson I.-M., Tarkowski A., Kokai-Kun J.F.,
RA   Mond J.J., Foster S.J.;
RT   "Catalase (katA) and alkyl hydroperoxide reductase (ahpC) have
RT   compensatory roles in peroxide stress resistance and are required for
RT   survival, persistence and nasal colonization in Staphylococcus
RT   aureus.";
RL   J. Bacteriol. 189:1025-1035(2007).
CC   -!- FUNCTION: Directly reduces organic hydroperoxides in its reduced
CC       dithiol form. Possesses broad-spectrum activity, being involved in
CC       hydrogen peroxide, cumene hydroperoxide, tert-butyl hydroperoxide,
CC       paraquat and peroxynitrite resistance. Is important for survival
CC       under desiccation conditions. Not required for virulence although
CC       is necessary for nasal colonization.
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   -!- INDUCTION: Induced by iron and osmotic shock. Repressed under
CC       metal-depleted growth conditions and by manganese-rich growth
CC       conditions. Negatively regulated by the ferric uptake regulator
CC       (fur) and perR.
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   -!- MISCELLANEOUS: In S.aureus, the removal of hydrogen peroxide
CC       appears to occur predominately via katA, with ahpC acting as an
CC       alternative.
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; U92441; AAB51151.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD29531.1; -; Genomic_DNA.
DR   PIR; S52934; S52934.
DR   RefSeq; YP_498954.1; -.
DR   HSSP; P19479; 1N8J.
DR   GeneID; 3919784; -.
DR   GenomeReviews; CP000253_GR; SAOUHSC_00365.
DR   KEGG; sao:SAOUHSC_00365; -.
DR   HOGENOM; P0A0B7; -.
DR   OMA; P0A0B7; GDLADHY.
DR   BioCyc; SAUR93061:SAOUHSC_00365-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; Direct protein sequencing;
KW   Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (Probable).
FT   CHAIN         2    189       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135128.
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).
FT   CONFLICT      2      2       S -> G (in Ref. 1; AA sequence).
FT   CONFLICT     17     17       D -> DD (in Ref. 1; AA sequence).
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
//