ID   AHPF_STAAW              Reviewed;         507 AA.
AC   P66013; Q99WJ7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF; OrderedLocusNames=MW0356;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000033; BAB94221.1; -; Genomic_DNA.
DR   RefSeq; WP_000930514.1; NC_003923.1.
DR   AlphaFoldDB; P66013; -.
DR   SMR; P66013; -.
DR   EnsemblBacteria; BAB94221; BAB94221; BAB94221.
DR   KEGG; sam:MW0356; -.
DR   HOGENOM; CLU_031864_4_2_9; -.
DR   OMA; VTVFEFM; -.
DR   Proteomes; UP000000418; Chromosome.
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: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.
FT   CHAIN           1..507
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166783"
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;  54708 MW;  6366693533CCD117 CRC64;
     MLNADLKQQL KQLLELMEGN VEFVASLGSD EKSKELKELL TEISDMSPRL SLSEKSLKRT
     PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KNLEGSFHFE
     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
     MSTGEEHLLN LDGIFVQIGL LPNTSWLKDA VELNERGEIV IDRNNNTNVP GIFAAGDVTD
     QKNKQIIISM GAGANAALNA FDYIIRN