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QOX1_STAES
ID   QOX1_STAES              Reviewed;         662 AA.
AC   Q8CPP7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable quinol oxidase subunit 1;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase polypeptide I;
GN   Name=qoxB; OrderedLocusNames=SE_0758;
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: Catalyzes quinol oxidation with the concomitant reduction of
CC       oxygen to water. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:132124;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds a copper B center. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=ferriheme a; Xref=ChEBI:CHEBI:60532; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Note=Heme A3. {ECO:0000250};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AE015929; AAO04355.1; -; Genomic_DNA.
DR   RefSeq; NP_764313.1; NC_004461.1.
DR   RefSeq; WP_001831713.1; NZ_WBME01000028.1.
DR   AlphaFoldDB; Q8CPP7; -.
DR   SMR; Q8CPP7; -.
DR   STRING; 176280.SE_0758; -.
DR   EnsemblBacteria; AAO04355; AAO04355; SE_0758.
DR   GeneID; 50019102; -.
DR   KEGG; sep:SE_0758; -.
DR   PATRIC; fig|176280.10.peg.730; -.
DR   eggNOG; COG0843; Bacteria.
DR   HOGENOM; CLU_011899_7_1_9; -.
DR   OMA; WAMMSIG; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR014233; QoxB.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   TIGRFAMs; TIGR02882; QoxB; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW   Ion transport; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..662
FT                   /note="Probable quinol oxidase subunit 1"
FT                   /id="PRO_0000276750"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        608..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         102
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         414
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        279..283
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   662 AA;  75267 MW;  6379B01B8D7C734D CRC64;
     MNFPWDQLLV KGNWMIISAQ IAAPFLVIGL IAVISYFKLW KYLYKEWFTS VDHKKIGIMY
     LISAVLMFVR GGIDALMLRT QLTIPDNKFL EANHYNEVFT THGVIMIIFM AMPFIFGLWN
     VVIPLQLGAR DVAFPVMNNV SFWLFFAGMI LFNLSFIVGG SPAAGWTNYA PLAGEFSPGP
     GVNYYLIAIQ ISGIGSLMTG INFFVTILRC KTPTMKFMQM PMFSVTTFIT TLIVILAFPV
     FTVALALMTA DRIFGTQFFT VANGGMPMLW ANFFWVWGHP EVYIVILPAF GMYSEIIPTF
     ARKRLFGHQS MIWATAGIAF LSFLVWVHHF FTMGNGALIN SFFSISTMLI GVPTGVKLFN
     WLLTLYKGRI TFESPMLFSL AFIPNFLLGG VTGVMLAMAS ADYQYHNTYF LVAHFHYTLV
     TGVVFACLAG LIFWYPKMMG YKLNETLNKW CFWFFMIGFN VCFLPQFILG LDGMPRRLYT
     YMPSDGWWLL NFISTIGAVL MAIGFLFLVA SIVYSHIKAP REATGDNWDG LGRTLEWSTA
     SAIPPKYNFA ITPDWNDYDT FVDMKEHGRH YLDNHNYKDI HMPNNTPVGF WMGIFMTIGG
     FFLIFESIVP ALICLAGIFI TMIWRSFQID HGYHIPASEV AETEARLREA RIKEREAVSH
     ES
 
 
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