ID   AHPF_STAA8              Reviewed;         507 AA.
AC   O05204; Q2G0Z7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF; OrderedLocusNames=SAOUHSC_00364;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Jones E.C., Francis K.P., Stewart G.S.A.B.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC       hydroperoxides. It can use either NADH or NADPH as electron donor for
CC       direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC       with the AhpC protein (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; U92441; AAB51152.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD29530.1; -; Genomic_DNA.
DR   RefSeq; WP_000930486.1; NZ_LS483365.1.
DR   RefSeq; YP_498953.1; NC_007795.1.
DR   AlphaFoldDB; O05204; -.
DR   SMR; O05204; -.
DR   STRING; 1280.SAXN108_0430; -.
DR   EnsemblBacteria; ABD29530; ABD29530; SAOUHSC_00364.
DR   GeneID; 3919783; -.
DR   KEGG; sao:SAOUHSC_00364; -.
DR   PATRIC; fig|93061.5.peg.334; -.
DR   eggNOG; COG3634; Bacteria.
DR   HOGENOM; CLU_031864_4_2_9; -.
DR   OMA; VTVFEFM; -.
DR   PRO; PR:O05204; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR   CDD; cd03026; AhpF_NTD_C; 1.
DR   CDD; cd02974; AhpF_NTD_N; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR044141; AhpF_NTD_C.
DR   InterPro; IPR044142; AhpF_NTD_N.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR03140; AhpF; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166784"
FT   BINDING         207..222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         347..361
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         467..477
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..338
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   507 AA;  54721 MW;  EDED04232731D21E CRC64;
     MLNADLKQQL KQLLELMEGN VEFVASLGSD DKSKELKDLL TEITDMSPRL SLSEKSLKRT
     PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KKLEGSFHFE
     TFISLTCQKC PDVVQALNLM SVINPNITHS MIDGAVFREE SENIMAVPAV FLNGEEFGNG
     RMTIQDILSK LGSTADASEF ENKEPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG
     QVNDTAGIEN FITVKETTGS EFSSNLAAHI DQYDIDAMTG IRATDIEKTD EAIKVTLENG
     AVLESKTVII ATGAGWRKLN IPGEEQLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA
     AIDLAGIVNH VTLFEFASEL KADNVLQDRL RSLSNVDIKT NAKTTEVVGE DHVTGIRYED
     MNTGEEHLLN LDGIFVQIGL LPNTSWLNDA VELNERGEIV IDRNNNTNVP GIFAAGDVTD
     QKNKQIIISM GAGANAALNA FDYIIRN