ID   QOX2_BACCR              Reviewed;         291 AA.
AC   Q81HT3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
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:0000250|UniProtKB:Q81V01}; OrderedLocusNames=BC_0698;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 29-47, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 14579 / DSM 31 / PYM1 {ECO:0000269|PubMed:12805383};
RX   PubMed=12805383; DOI=10.1074/jbc.m302583200;
RA   Contreras-Zentella M., Mendoza G., Membrillo-Hernandez J., Escamilla J.E.;
RT   "A novel double heme substitution produces a functional bo3 variant of the
RT   quinol oxidase aa3 of Bacillus cereus. Purification and partial
RT   characterization.";
RL   J. Biol. Chem. 278:31473-31478(2003).
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.
CC       {ECO:0000269|PubMed:12805383, ECO:0000305}.
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:0000269|PubMed:12805383};
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; AE016877; AAP07712.1; -; Genomic_DNA.
DR   RefSeq; NP_830511.1; NC_004722.1.
DR   RefSeq; WP_001176165.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81HT3; -.
DR   SMR; Q81HT3; -.
DR   STRING; 226900.BC_0698; -.
DR   MetOSite; Q81HT3; -.
DR   EnsemblBacteria; AAP07712; AAP07712; BC_0698.
DR   GeneID; 67505396; -.
DR   KEGG; bce:BC0698; -.
DR   PATRIC; fig|226900.8.peg.658; -.
DR   HOGENOM; CLU_036876_6_0_9; -.
DR   OMA; TAMNSFF; -.
DR   Proteomes; UP000001417; 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; IDA:UniProtKB.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Electron transport; Membrane;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:12805383"
FT   CHAIN           29..291
FT                   /note="Quinol oxidase subunit 2"
FT                   /id="PRO_0000006068"
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;  33293 MW;  D77FCA248374AD4F CRC64;
     MQLKKAFWKL ASLLPLSLLL FLGGCDKKLA VLNPQGPVAK AQYDLIVWSF LLMSLIIAIV
     FILFTVILIR YREKPENMDY EPPEQHGNTL LEIIWTLVPV IIVIALSIPT VKATYASEEV
     PKESKHIKPV EIYVTSANWK WLFSYPEEKI ETVNYLNIPA GVPIQFKLTS VGPMNAFWVP
     ELGGMKYTMD GMIMDLYLQA DKPGSYLGRS ANFSGEGFTH MEFEVEAKTK EKYDKWVKEV
     QETAPKLTEA KYNEIVKPGV VGRMTFSSHH LSYVDPKSLE YCDYNYYKNK K