ID   AHPF_STAES              Reviewed;         507 AA.
AC   Q8CMQ1;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
GN   Name=ahpF; OrderedLocusNames=SE_2358;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO06001.1; -; Genomic_DNA.
DR   RefSeq; NP_765913.1; NC_004461.1.
DR   RefSeq; WP_001829382.1; NZ_WBME01000004.1.
DR   AlphaFoldDB; Q8CMQ1; -.
DR   SMR; Q8CMQ1; -.
DR   STRING; 176280.SE_2358; -.
DR   EnsemblBacteria; AAO06001; AAO06001; SE_2358.
DR   KEGG; sep:SE_2358; -.
DR   PATRIC; fig|176280.10.peg.2301; -.
DR   eggNOG; COG3634; Bacteria.
DR   HOGENOM; CLU_031864_4_2_9; -.
DR   OMA; VTVFEFM; -.
DR   Proteomes; UP000001411; 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; 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_0000166785"
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;  54670 MW;  C95C637261C5F571 CRC64;
     MLNADLKQQL QQLLELMEGD VEFVASLGSD DKSNELKELL NEIAEMSAHI TITEKSLKRT
     PSFSVNRPGE ETGITFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KGLEGPFHFE
     TFVSLTCQKC PDVVQALNLM SVINPNITHT MIDGAVFREE SENIMAVPAV FLDGQEFGNG
     RMTVQDILTK LGSTQDASEF NDKDPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG
     QVNDTAGIEN FITVKETTGS EFSSNLAEHI AQYDIDTMTG IRATNIEKTD SAIRVTLEND
     AVLESKTVII STGASWRKLN IPGEDRLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA
     AIDLAGIVKH VTLFEYASEL KADSVLQERL RSLPNVDIKT SAKTTEVIGD DYVTGISYED
     MTTGESQVVN LDGIFVQIGL VPNTSWLQNA VELNERGEVM INRDNATNVP GIFAAGDVTD
     QKNKQIIISM GAGANAALNA FDYIIRN