ID   QOX4_STAAS              Reviewed;          96 AA.
AC   Q6GAF5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Probable quinol oxidase subunit 4;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase polypeptide IV;
GN   Name=qoxD; OrderedLocusNames=SAS0993;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit 4
CC       family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG42768.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GAF5; -.
DR   SMR; Q6GAF5; -.
DR   KEGG; sas:SAS0993; -.
DR   HOGENOM; CLU_140945_2_0_9; -.
DR   OMA; AASIWIM; -.
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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR005171; Cyt_c_oxidase_su4_prok.
DR   InterPro; IPR014250; QoxD.
DR   Pfam; PF03626; COX4_pro; 1.
DR   TIGRFAMs; TIGR02901; QoxD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..96
FT                   /note="Probable quinol oxidase subunit 4"
FT                   /id="PRO_0000275860"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   96 AA;  10687 MW;  614E29CDB8BE3EAE CRC64;
     MSTIMKHTVG FIASIVLTLL AVYVTLYTSL TFHAKLTIIF GFAFVQAGLQ LLMFMHLTEG
     KDGRLQTFKV IFALVITLCF VVGTYWVMQG GHSSHL