ID   QOX3_STAAW              Reviewed;         201 AA.
AC   Q7A183;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Probable quinol oxidase subunit 3;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase polypeptide III;
GN   Name=qoxC; OrderedLocusNames=MW0942;
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: 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 subunit 3 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB94807.1; -; Genomic_DNA.
DR   RefSeq; WP_000017736.1; NC_003923.1.
DR   AlphaFoldDB; Q7A183; -.
DR   SMR; Q7A183; -.
DR   EnsemblBacteria; BAB94807; BAB94807; BAB94807.
DR   GeneID; 66839255; -.
DR   KEGG; sam:MW0942; -.
DR   HOGENOM; CLU_044071_3_2_9; -.
DR   OMA; SIYWWGS; -.
DR   Proteomes; UP000000418; 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:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd02863; Ubiquinol_oxidase_III; 1.
DR   Gene3D; 1.20.120.80; -; 1.
DR   InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR   InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR   InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   InterPro; IPR014246; QoxC.
DR   InterPro; IPR033946; Ubiquinol_oxase_su3_dom.
DR   PANTHER; PTHR11403; PTHR11403; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; SSF81452; 1.
DR   TIGRFAMs; TIGR02897; QoxC; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..201
FT                   /note="Probable quinol oxidase subunit 3"
FT                   /id="PRO_0000275889"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   201 AA;  23057 MW;  0DBD36DE9ED6E758 CRC64;
     MSHDTNTIDS RTHEGELNKL GFWIFITAEF ALFGTLFATL LTLQHGGDYA GKMTTELFEL
     PLVLIMTFAL LFSSYTCGIA IYYMRQEKQK LMMFWMIITL LLGLVFVGFE IYEFAHYASE
     GVNPTIGSYW SSFFILLGTH GCHVSLGIVW AICLLIQIQR RGLDKYNAPK LFIVSLYWHF
     LDVVWVFIFT AVYMIGMVYS G