ID   QOX3_STAAM              Reviewed;         201 AA.
AC   Q99V38;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable quinol oxidase subunit 3;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase polypeptide III;
GN   Name=qoxC; OrderedLocusNames=SAV1059;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57221.1; -; Genomic_DNA.
DR   RefSeq; WP_000017736.1; NC_002758.2.
DR   AlphaFoldDB; Q99V38; -.
DR   SMR; Q99V38; -.
DR   PaxDb; Q99V38; -.
DR   EnsemblBacteria; BAB57221; BAB57221; SAV1059.
DR   GeneID; 66839255; -.
DR   KEGG; sav:SAV1059; -.
DR   HOGENOM; CLU_044071_3_2_9; -.
DR   OMA; SIYWWGS; -.
DR   PhylomeDB; Q99V38; -.
DR   BioCyc; SAUR158878:SAV_RS05710-MON; -.
DR   Proteomes; UP000002481; 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_0000275888"
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