ID   QOX4_BACSU              Reviewed;         124 AA.
AC   P34959;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 120.
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=BSU38140; ORFNames=ipa-40d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1316894; DOI=10.1016/s0021-9258(19)50007-2;
RA   Santana M., Kunst F., Hullo M.-F., Rapoport G., Danchin A., Glaser P.;
RT   "Molecular cloning, sequencing, and physiological characterization of the
RT   qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase.";
RL   J. Biol. Chem. 267:10225-10231(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC       oxygen to water. Major component for energy conversion during
CC       vegetative growth (By similarity). {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:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit 4
CC       family. {ECO:0000305}.
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DR   EMBL; M86548; AAA22689.1; -; Genomic_DNA.
DR   EMBL; X73124; CAA51596.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15840.1; -; Genomic_DNA.
DR   PIR; D38129; D38129.
DR   RefSeq; NP_391693.1; NC_000964.3.
DR   RefSeq; WP_003227410.1; NZ_JNCM01000034.1.
DR   PDB; 6KOB; X-ray; 3.60 A; D/H=48-124.
DR   PDB; 6KOC; X-ray; 3.80 A; D/H=48-124.
DR   PDB; 6KOE; X-ray; 3.75 A; D/H=48-124.
DR   PDBsum; 6KOB; -.
DR   PDBsum; 6KOC; -.
DR   PDBsum; 6KOE; -.
DR   AlphaFoldDB; P34959; -.
DR   SMR; P34959; -.
DR   STRING; 224308.BSU38140; -.
DR   PaxDb; P34959; -.
DR   EnsemblBacteria; CAB15840; CAB15840; BSU_38140.
DR   GeneID; 937285; -.
DR   KEGG; bsu:BSU38140; -.
DR   PATRIC; fig|224308.179.peg.4128; -.
DR   eggNOG; COG3125; Bacteria.
DR   InParanoid; P34959; -.
DR   OMA; IVVHMVF; -.
DR   PhylomeDB; P34959; -.
DR   BioCyc; BSUB:BSU38140-MON; -.
DR   BioCyc; MetaCyc:BSU38140-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IBA:GO_Central.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:UniProtKB.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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   3D-structure; Cell membrane; Membrane; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..124
FT                   /note="Quinol oxidase subunit 4"
FT                   /id="PRO_0000183903"
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;  13687 MW;  09993B334926819D CRC64;
     MANKSAEHSH FPWKHIVGFI LSIVLTLLAL WVAVYTDLSS SAKLWIIFGF AFIQAALQLL
     MFMHMTESEN GTIQVGNTLF GFFGAIVIVL GSIWIFAAHY HHGDHMDGNP PGGAEHSEHS
     GHNE