ID   QOX4_BACSH              Reviewed;         124 AA.
AC   E0TW64;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Quinol oxidase subunit 4;
DE            EC=1.10.3.-;
DE   AltName: Full=Quinol oxidase aa3-600, subunit qoxD;
DE   AltName: Full=Quinol oxidase polypeptide IV;
GN   Name=qoxD; OrderedLocusNames=BSUW23_18860;
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 2-17, 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.
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 bacterial subunit 4
CC       family. {ECO:0000305}.
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DR   EMBL; CP002183; ADM39806.1; -; Genomic_DNA.
DR   RefSeq; WP_003222169.1; NC_014479.1.
DR   AlphaFoldDB; E0TW64; -.
DR   SMR; E0TW64; -.
DR   EnsemblBacteria; ADM39806; ADM39806; BSUW23_18860.
DR   GeneID; 64305588; -.
DR   KEGG; bss:BSUW23_18860; -.
DR   HOGENOM; CLU_140945_2_0_9; -.
DR   OMA; IVVHMVF; -.
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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR005171; Cyt_c_oxidase_su4_prok.
DR   InterPro; IPR014250; QoxD.
DR   Pfam; PF03626; COX4_pro; 1.
DR   TIGRFAMs; TIGR02901; QoxD; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Membrane; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7575098"
FT   CHAIN           2..124
FT                   /note="Quinol oxidase subunit 4"
FT                   /id="PRO_0000402832"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   124 AA;  13601 MW;  C01999B97FA2DA46 CRC64;
     MANKSAEHSH FPWKHIVGFA LSIVLTLLAL WVAVYTDLSS SAKLWIIFGF AFIQAALQLL
     MFMHMTESEN GGIQVGNTLF GFFGAIVIVL GSIWIFAAHY HHGDHMDGNP PGGAEHSEHS
     GHNE