ID   QOX2_BACC1              Reviewed;         291 AA.
AC   Q73DE0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Quinol oxidase subunit 2;
DE            EC=1.10.3.-;
DE   AltName: Full=Cytochrome aa(3) subunit 2;
DE   AltName: Full=Quinol oxidase polypeptide II;
DE   Flags: Precursor;
GN   Name=qoxA {ECO:0000312|EMBL:AAS39705.1}; OrderedLocusNames=BCE_0772;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(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|UniProtKB:Q81HT3}.
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; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000255}.
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DR   EMBL; AE017194; AAS39705.1; -; Genomic_DNA.
DR   RefSeq; WP_001176169.1; NC_003909.8.
DR   PRIDE; Q73DE0; -.
DR   EnsemblBacteria; AAS39705; AAS39705; BCE_0772.
DR   KEGG; bca:BCE_0772; -.
DR   HOGENOM; CLU_036876_6_0_9; -.
DR   OMA; TAMNSFF; -.
DR   Proteomes; UP000002527; 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; IPR006333; Cyt_o_ubiquinol_oxidase_su2.
DR   InterPro; IPR006332; QoxA.
DR   PANTHER; PTHR22888; PTHR22888; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   PIRSF; PIRSF000292; Ubi_od_II; 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.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Membrane; Oxidoreductase;
KW   Respiratory chain; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250|UniProtKB:Q81HT3"
FT   CHAIN           29..291
FT                   /note="Quinol oxidase subunit 2"
FT                   /id="PRO_0000006067"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   291 AA;  33334 MW;  1BF568A873B56D40 CRC64;
     MQLKKAFWKL ASLLPXSLLL FLGGCDKKLA VLNPQGPVAK AQYDLIVWSF LLMSLIIAIV
     FILFTVILIR YREKPENMDY EPPEQHGNTL LEIIWTLVPV IIVIALSIPT VKATYASEEV
     PKESKHIKPV EIYVTSANWK WLFSYPEEKI ETVNYLNIPA GVPIQFKLTS VGPMNAFWVP
     ELGGMKYTMD GMIMDLYLQA DKPGSYLGRS ANFSGEGFTH MEFEVEAKTK EKYDKWVKEV
     QQTAPKLTED KYNEIVKPGV VGRMTFSSHH LSYVDPKSLE YCDYNYYKNK K