ID   QOX2_BACSH              Reviewed;         321 AA.
AC   E0TW67;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Quinol oxidase subunit 2;
DE            EC=1.10.3.-;
DE   AltName: Full=Oxidase aa(3)-600 subunit 2;
DE   AltName: Full=Quinol oxidase aa3-600, subunit qoxA;
DE   AltName: Full=Quinol oxidase polypeptide II;
DE   Flags: Precursor;
GN   Name=qoxA; OrderedLocusNames=BSUW23_18875;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-42, AND CHARACTERIZATION.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=7575098; DOI=10.1007/bf00272132;
RA   Lemma E., Simon J., Schagger H., Kroger A.;
RT   "Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of
RT   Bacillus subtilis.";
RL   Arch. Microbiol. 163:432-438(1995).
CC   -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC       oxygen to water. Major component for energy conversion during
CC       vegetative growth. Subunit II transfers the electrons from a quinol to
CC       the binuclear center of the catalytic subunit I.
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; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADM39809.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002183; ADM39809.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; E0TW67; -.
DR   SMR; E0TW67; -.
DR   EnsemblBacteria; ADM39809; ADM39809; BSUW23_18875.
DR   KEGG; bss:BSUW23_18875; -.
DR   HOGENOM; CLU_036876_6_0_9; -.
DR   Proteomes; UP000002233; 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; PF00116; COX2; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Electron transport; Lipoprotein;
KW   Membrane; Oxidoreductase; Palmitate; Respiratory chain; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:7575098"
FT   CHAIN           26..321
FT                   /note="Quinol oxidase subunit 2"
FT                   /id="PRO_0000402830"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          294..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   321 AA;  36255 MW;  C1FA19F54FE8160C CRC64;
     MIFLFRALKP LLVLALLTVV FVLGGCSNAS VLDPKGPVAE QQSDLILLSI GFMLFIVGVV
     FVLFTIILVK YRDRKGKDNG SYNPKIHGNT FLEVVWTVIP ILIVIALSVP TVQTIYSLEK
     APEATKDKEP LVVHATSVDW KWVFSYPEQD IETVNYLNIP VDRPILFKIS SADSMASLWI
     PQLGGQKYAM AGMLMDQYLQ ADEVGTYQGR NANFTGEHFA DQEFDVNAVT EKDFNSWVKK
     TQNEAPKLTK EKYDQLMLPE NVDELTFSST HLKYVDHGQD AEYAMEARKR LGYQAVSPHS
     KTDPFENVKE NEFKKSDDTE E