QOX2_STAAR
ID QOX2_STAAR Reviewed; 366 AA.
AC Q6GI23;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Probable quinol oxidase subunit 2;
DE EC=1.10.3.-;
DE AltName: Full=Quinol oxidase polypeptide II;
DE Flags: Precursor;
GN Name=qoxA; OrderedLocusNames=SAR1034;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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. Subunit II transfers the electrons from a quinol to
CC the binuclear center of the catalytic subunit I (By similarity).
CC {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:0000255|PROSITE-
CC ProRule:PRU00303}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; BX571856; CAG40038.1; -; Genomic_DNA.
DR RefSeq; WP_000032836.1; NC_002952.2.
DR AlphaFoldDB; Q6GI23; -.
DR SMR; Q6GI23; -.
DR KEGG; sar:SAR1034; -.
DR HOGENOM; CLU_036876_6_0_9; -.
DR OMA; TAMNSFF; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000000596; 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:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR CDD; cd04212; CuRO_UO_II; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034227; CuRO_UO_II.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR InterPro; IPR006332; QoxA.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR01432; QOXA; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Lipoprotein; Membrane; Oxidoreductase;
KW Palmitate; Respiratory chain; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..366
FT /note="Probable quinol oxidase subunit 2"
FT /id="PRO_0000275873"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 330..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 366 AA; 41777 MW; D3200D588A7BF1DF CRC64;
MSKFKSLLLL FGTLILLSGC SNIEIFNAKG PVASSQKFLI LYSIVFMLVI CFVVLGMFAI
FIYKYSYNKN AESGKMHHNA IIETIWFVIP IIIVAALAIP TVKTLYDYEK PPKSEKDPMV
VYAVSAGYKW FFAYPDEHIE TVNTLTIPKD RPVVFKLQAM DTMTSFWIPQ LGGQKYAMTG
MTMNWTLEAS QTGTFRGRNS NFNGEGFSRQ TFKVNAVSQK DYDKWVKEVK GKKTLDQDTF
DKQLLPSTPN KALEFNGTHM AFVDPAADPE YIFYAYKRFN FELKDPNFTS EENMFKDVSD
KPLIPARKAQ ITNANYKRHG MKLMILGNDE PYNNEFKKDE SKNAKEMKKI SKDAQDQDND
DHGGGH