QOX3_STAHJ
ID QOX3_STAHJ Reviewed; 201 AA.
AC Q4L563;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Probable quinol oxidase subunit 3;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide III;
GN Name=qoxC; OrderedLocusNames=SH1903;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05212.1; -; Genomic_DNA.
DR RefSeq; WP_011276175.1; NC_007168.1.
DR AlphaFoldDB; Q4L563; -.
DR SMR; Q4L563; -.
DR STRING; 279808.SH1903; -.
DR EnsemblBacteria; BAE05212; BAE05212; SH1903.
DR GeneID; 58061980; -.
DR KEGG; sha:SH1903; -.
DR eggNOG; COG1845; Bacteria.
DR HOGENOM; CLU_044071_3_2_9; -.
DR OMA; SIYWWGS; -.
DR OrthoDB; 1502742at2; -.
DR Proteomes; UP000000543; 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_0000275895"
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; 22909 MW; 3D86FDD48A37B295 CRC64;
MSHDTNTVDS RTHEGQLNKL GFWIFLTAEF SLFGTLFATL LTLQHGGDYA GKMTTELFEL
PLVLIMTFAL LISSYTCGIS IYYMRKEKQN LMMFWMILTV LLGLVFVGFE IYEFAHYVSE
GVTPQIGSYW SSFFILLGTH GAHVSLGIGW IICLLIQVAT RGLNKYNAPK LFIVSLYWHF
LDVVWIFIFT AVYMIGMVYS G