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Database: UniProt
Entry: P34956
LinkDB: P34956
Original site: P34956 
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   03-SEP-2014, entry version 119.
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; FLILCYN; -.
DR   OrthoDB; EOG6B35XR; -.
DR   PhylomeDB; P34956; -.
DR   BioCyc; BSUB:BSU38160-MONOMER; -.
DR   BioCyc; MetaCyc:BSU38160-MONOMER; -.
DR   UniPathway; UPA00705; -.
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: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: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; IPR000883; COX1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR   InterPro; IPR014233; QoxB.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 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
//
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