QOX2_STAS1
ID QOX2_STAS1 Reviewed; 373 AA.
AC Q49WI4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=SSP1730;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18875.1; -; Genomic_DNA.
DR RefSeq; WP_011303443.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49WI4; -.
DR SMR; Q49WI4; -.
DR STRING; 342451.SSP1730; -.
DR EnsemblBacteria; BAE18875; BAE18875; SSP1730.
DR KEGG; ssp:SSP1730; -.
DR PATRIC; fig|342451.11.peg.1729; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_6_0_9; -.
DR OMA; TAMNSFF; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000006371; 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; Reference proteome; Respiratory chain; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..373
FT /note="Probable quinol oxidase subunit 2"
FT /id="PRO_0000275883"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 292..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
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 373 AA; 42665 MW; 0519A00955824123 CRC64;
MSKFKSLLLL FGSLILLSGC SNVEVLNPKG PMASDSKFLI MYSIIFMLVI IAAVLILFTV
FLYKYRIGNT DESGKMHHNS LLETIWFIIP VIIVIALAIP TVNSLYNYEE KPQKEDDPLV
VYATSAGYKW FFSYPEEKIE TVNHLTIPKD RPVVFKLQSM DMMTSFWIPQ LGGQKYAMTG
MTMDWTLTAS EEGTFRGRNS NFNGEGFSRQ TFDVNSVSQS KFEDWVKDAK KQKVLDQDTF
DKQLLPTTEN KNLTFSGTHL AFVDPAADPE YIFYAYDRYN FVQKDPNFNT EEERTADVLD
KPDQPARKPE ITNANYERHG MKAMILGNNE PYDSEFKDEE SHNMDEMEKI SEGAKDEKAS
KIEKKDHENG GGH