ID QOX1_BACSU Reviewed; 649 AA.
AC P34956;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 01-MAY-2013, entry version 111.
DE RecName: Full=Quinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Oxidase aa(3)-600 subunit 1;
DE AltName: Full=Quinol oxidase aa3-600, subunit QoxB;
DE AltName: Full=Quinol oxidase polypeptide I;
GN Name=qoxB; OrderedLocusNames=BSU38160; ORFNames=ipa-38d;
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;
RA Santana M., Kunst F., Hullo M.-F., Rapoport G., Danchin A., Glaser P.;
RT "Molecular cloning, sequencing, and physiological characterization of
RT the qox operon from Bacillus subtilis encoding the aa3-600 quinol
RT 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.,
RA Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I.,
RA Presecan E., Santana M., Schneider E., Schweizer J., Vertes A.,
RA 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.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA 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.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA 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
CC reduction of oxygen to water. Major component for energy
CC conversion during vegetative growth (By similarity).
CC -!- CATALYTIC ACTIVITY: Ubiquinol-8 + O(2) = Ubiquinone-8 + H(2)O.
CC -!- COFACTOR: Copper B (By similarity).
CC -!- COFACTOR: Heme A (By similarity).
CC -!- COFACTOR: Heme A3 (By similarity).
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR EMBL; M86548; AAA22687.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51594.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15842.1; -; Genomic_DNA.
DR PIR; B38129; B38129.
DR RefSeq; NP_391695.1; NC_000964.3.
DR ProteinModelPortal; P34956; -.
DR SMR; P34956; 51-549.
DR STRING; 224308.BSU38160; -.
DR PaxDb; P34956; -.
DR EnsemblBacteria; CAB15842; CAB15842; BSU38160.
DR GeneID; 937303; -.
DR KEGG; bsu:BSU38160; -.
DR PATRIC; 18979676; VBIBacSub10457_4000.
DR GenoList; BSU38160; -.
DR eggNOG; COG0843; -.
DR HOGENOM; HOG000085275; -.
DR KO; K02827; -.
DR OMA; KKIHMPS; -.
DR ProtClustDB; CLSK2459908; -.
DR BioCyc; BSUB:BSU38160-MONOMER; -.
DR BioCyc; MetaCyc:BSU38160-MONOMER; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR014233; Cyt_aa3_quinol_oxidase_su1.
DR InterPro; IPR000883; Cyt_c_Oxase_su1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; COX1; 1.
DR TIGRFAMs; TIGR02882; QoxB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Complete proteome; Copper; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 649 Quinol oxidase subunit 1.
FT /FTId=PRO_0000183474.
FT TOPO_DOM 1 15 Extracellular (Potential).
FT TRANSMEM 16 34 Helical; (Potential).
FT TOPO_DOM 35 56 Cytoplasmic (Potential).
FT TRANSMEM 57 75 Helical; (Potential).
FT TOPO_DOM 76 97 Extracellular (Potential).
FT TRANSMEM 98 117 Helical; (Potential).
FT TOPO_DOM 118 139 Cytoplasmic (Potential).
FT TRANSMEM 140 157 Helical; (Potential).
FT TOPO_DOM 158 190 Extracellular (Potential).
FT TRANSMEM 191 209 Helical; (Potential).
FT TOPO_DOM 210 227 Cytoplasmic (Potential).
FT TRANSMEM 228 246 Helical; (Potential).
FT TOPO_DOM 247 272 Extracellular (Potential).
FT TRANSMEM 273 292 Helical; (Potential).
FT TOPO_DOM 293 315 Cytoplasmic (Potential).
FT TRANSMEM 316 335 Helical; (Potential).
FT TOPO_DOM 336 343 Extracellular (Potential).
FT TRANSMEM 344 362 Helical; (Potential).
FT TOPO_DOM 363 377 Cytoplasmic (Potential).
FT TRANSMEM 378 397 Helical; (Potential).
FT TOPO_DOM 398 405 Extracellular (Potential).
FT TRANSMEM 406 425 Helical; (Potential).
FT TOPO_DOM 426 452 Cytoplasmic (Potential).
FT TRANSMEM 453 472 Helical; (Potential).
FT TOPO_DOM 473 490 Extracellular (Potential).
FT TRANSMEM 491 510 Helical; (Potential).
FT TOPO_DOM 511 584 Cytoplasmic (Potential).
FT TRANSMEM 585 604 Helical; (Potential).
FT TOPO_DOM 605 610 Extracellular (Potential).
FT TRANSMEM 611 631 Helical; (Potential).
FT TOPO_DOM 632 649 Cytoplasmic (Potential).
FT METAL 102 102 Iron (heme A axial ligand) (By
FT similarity).
FT METAL 280 280 Copper B (By similarity).
FT METAL 284 284 Copper B (By similarity).
FT METAL 329 329 Copper B (By similarity).
FT METAL 330 330 Copper B (By similarity).
FT METAL 415 415 Iron (heme A3 axial ligand) (By
FT similarity).
FT METAL 417 417 Iron (heme A axial ligand) (By
FT similarity).
FT CROSSLNK 280 284 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
SQ SEQUENCE 649 AA; 73838 MW; 5D77F58ED64CBFCC CRC64;
MKFKWDEFFV TGDPLILGAQ VSIALSTIAI IFVLTYFKKW KWLWSEWITT VDHKKLGIMY
IISAVIMLFR GGVDGLMMRA QLALPNNSFL DSNHYNEIFT THGTIMIIFM AMPFLIGLIN
VVVPLQIGAR DVAFPYLNNL SFWTFFVGAM LFNISFVIGG SPNAGWTSYM PLASNDMSPG
PGENYYLLGL QIAGIGTLMT GINFMVTILK MRTKGMTLMR MPMFTWTTLI TMVIIVFAFP
VLTVALALLS FDRLFGAHFF TLEAGGMPML WANLFWIWGH PEVYIVILPA FGIFSEIISS
FARKQLFGYK AMVGSIIAIS VLSFLVWTHH FFTMGNSASV NSFFSITTMA ISIPTGVKIF
NWLFTMYKGR ISFTTPMLWA LAFIPNFVIG GVTGVMLAMA AADYQYHNTY FLVSHFHYVL
IAGTVFACFA GFIFWYPKMF GHKLNERIGK WFFWIFMIGF NICFFPQYFL GLQGMPRRIY
TYGPNDGWTT LNFISTVGAF MMGVGFLILC YNIYYSFRYS TREISGDSWG VGRTLDWATS
SAIPPHYNFA VLPEVKSQDA FLHMKEEKTE LYPESKFKKI HMPSNSGRPF FMSVAFGLAG
FGLVFEWYWM GVVGLIGVLL CMVLRSFEYD NGYYISVDEI KETERKISE
//
