QOX3_BACSU
ID QOX3_BACSU Reviewed; 204 AA.
AC P34958;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Quinol oxidase subunit 3;
DE EC=1.10.3.-;
DE AltName: Full=Oxidase aa(3)-600 subunit 3;
DE AltName: Full=Quinol oxidase aa3-600, subunit QoxC;
DE AltName: Full=Quinol oxidase polypeptide III;
GN Name=qoxC; OrderedLocusNames=BSU38150; ORFNames=ipa-39d;
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 subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; M86548; AAA22688.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51595.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15841.1; -; Genomic_DNA.
DR PIR; C38129; C38129.
DR RefSeq; NP_391694.1; NC_000964.3.
DR RefSeq; WP_003227409.1; NZ_JNCM01000034.1.
DR PDB; 6KOB; X-ray; 3.60 A; C/G=1-204.
DR PDB; 6KOC; X-ray; 3.80 A; C/G=1-204.
DR PDB; 6KOE; X-ray; 3.75 A; C/G=1-204.
DR PDBsum; 6KOB; -.
DR PDBsum; 6KOC; -.
DR PDBsum; 6KOE; -.
DR AlphaFoldDB; P34958; -.
DR SMR; P34958; -.
DR STRING; 224308.BSU38150; -.
DR jPOST; P34958; -.
DR PaxDb; P34958; -.
DR PRIDE; P34958; -.
DR EnsemblBacteria; CAB15841; CAB15841; BSU_38150.
DR GeneID; 937299; -.
DR KEGG; bsu:BSU38150; -.
DR PATRIC; fig|224308.179.peg.4129; -.
DR eggNOG; COG1845; Bacteria.
DR InParanoid; P34958; -.
DR OMA; SIYWWGS; -.
DR PhylomeDB; P34958; -.
DR BioCyc; BSUB:BSU38150-MON; -.
DR BioCyc; MetaCyc:BSU38150-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:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer 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:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; 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 CDD; cd02863; Ubiquinol_oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR InterPro; IPR014246; QoxC.
DR InterPro; IPR033946; Ubiquinol_oxase_su3_dom.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR TIGRFAMs; TIGR02897; QoxC; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..204
FT /note="Quinol oxidase subunit 3"
FT /id="PRO_0000183892"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 204 AA; 22672 MW; 987962635C1D106B CRC64;
MEHAEHGNSN APMEYQSETG RLNILGFWIF LGAEIVLFST LFATFFVLKN RTAGGVLPDE
LFEVNLVMIM TFLLLISSFT CGIAVHEMRR GSLKGVVIWT IITLLLGAGF VGCEINEFVH
YVHEGAALST SAFWSGFFVL LGTHGTHVTI GIFWITGILI QLKKRGLTPQ TSSKIFISSL
YWHFLDVVWI FIFTGVYLMG LGGL
