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Database: UniProt
Entry: Q8K994
LinkDB: Q8K994
Original site: Q8K994 
ID   CYOB_BUCAP              Reviewed;         659 AA.
AC   Q8K994;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   01-OCT-2014, entry version 97.
DE   RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1;
DE            EC=1.10.3.10;
DE   AltName: Full=Cytochrome o ubiquinol oxidase subunit 1;
DE            Short=Cytochrome o subunit 1;
DE   AltName: Full=Oxidase bo(3) subunit 1;
DE   AltName: Full=Ubiquinol oxidase polypeptide I;
DE   AltName: Full=Ubiquinol oxidase subunit 1;
GN   Name=cyoB; OrderedLocusNames=BUsg_455;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the
CC       component of the aerobic respiratory chain of E.coli that
CC       predominates when cells are grown at high aeration. Has proton
CC       pump activity across the membrane in addition to electron
CC       transfer, pumping 2 protons/electron (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 ubiquinol + O(2) + n H(+)(Side 1) = 2
CC       ubiquinone + 2 H(2)O + n H(+)(Side 2).
CC   -!- COFACTOR: Binds 1 copper B ion per subunit. {ECO:0000250}.
CC   -!- COFACTOR: Binds 1 low-spin heme b per subunit. {ECO:0000250}.
CC   -!- COFACTOR: Binds 1 high-spin heme o per subunit. {ECO:0000250}.
CC   -!- COFACTOR: Bind 1 high-affinity quinone that appears to function as
CC       a tightly bound cofactor (QH), forming a semiquinone intermediate
CC       in the reaction. {ECO:0000250}.
CC   -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains
CC       and two D chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in
CC       the electron transport chain.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67998.1; -; Genomic_DNA.
DR   RefSeq; NP_660787.1; NC_004061.1.
DR   ProteinModelPortal; Q8K994; -.
DR   SMR; Q8K994; 52-552.
DR   STRING; 198804.BUsg455; -.
DR   EnsemblBacteria; AAM67998; AAM67998; BUsg_455.
DR   GeneID; 1005710; -.
DR   KEGG; bas:BUsg455; -.
DR   PATRIC; 21247764; VBIBucAph100086_0481.
DR   eggNOG; COG0843; -.
DR   KO; K02298; -.
DR   OMA; FLILCYN; -.
DR   OrthoDB; EOG6B35XR; -.
DR   BioCyc; BAPH198804:GHMG-479-MONOMER; -.
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: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; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
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; IPR014207; Cyt_c_ubiqinol_oxidase_su1.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   TIGRFAMs; TIGR02843; CyoB; 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; Respiratory chain; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    659       Cytochrome bo(3) ubiquinol oxidase
FT                                subunit 1.
FT                                /FTId=PRO_0000183480.
FT   TOPO_DOM      1     14       Extracellular. {ECO:0000255}.
FT   TRANSMEM     15     35       Helical. {ECO:0000255}.
FT   TOPO_DOM     36     58       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     59     79       Helical. {ECO:0000255}.
FT   TOPO_DOM     80    106       Extracellular. {ECO:0000255}.
FT   TRANSMEM    107    127       Helical. {ECO:0000255}.
FT   TOPO_DOM    128    145       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    146    166       Helical. {ECO:0000255}.
FT   TOPO_DOM    167    189       Extracellular. {ECO:0000255}.
FT   TRANSMEM    190    210       Helical. {ECO:0000255}.
FT   TOPO_DOM    211    225       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    226    246       Helical. {ECO:0000255}.
FT   TOPO_DOM    247    277       Extracellular. {ECO:0000255}.
FT   TRANSMEM    278    298       Helical. {ECO:0000255}.
FT   TOPO_DOM    299    309       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    310    330       Helical. {ECO:0000255}.
FT   TOPO_DOM    331    347       Extracellular. {ECO:0000255}.
FT   TRANSMEM    348    368       Helical. {ECO:0000255}.
FT   TOPO_DOM    369    380       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    381    401       Helical. {ECO:0000255}.
FT   TOPO_DOM    402    413       Extracellular. {ECO:0000255}.
FT   TRANSMEM    414    434       Helical. {ECO:0000255}.
FT   TOPO_DOM    435    456       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    457    477       Helical. {ECO:0000255}.
FT   TOPO_DOM    478    490       Extracellular. {ECO:0000255}.
FT   TRANSMEM    491    511       Helical. {ECO:0000255}.
FT   TOPO_DOM    512    580       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    581    601       Helical. {ECO:0000255}.
FT   TOPO_DOM    602    605       Extracellular. {ECO:0000255}.
FT   TRANSMEM    606    626       Helical. {ECO:0000255}.
FT   TOPO_DOM    627    659       Cytoplasmic. {ECO:0000255}.
FT   METAL       106    106       Iron (heme b axial ligand).
FT                                {ECO:0000250}.
FT   METAL       284    284       Copper. {ECO:0000250}.
FT   METAL       288    288       Copper. {ECO:0000250}.
FT   METAL       333    333       Copper. {ECO:0000250}.
FT   METAL       334    334       Copper. {ECO:0000250}.
FT   METAL       419    419       Iron (heme o axial ligand).
FT                                {ECO:0000250}.
FT   METAL       421    421       Iron (heme b axial ligand).
FT                                {ECO:0000250}.
FT   BINDING      71     71       Quinone (QH). {ECO:0000250}.
FT   BINDING      75     75       Quinone (QH). {ECO:0000250}.
FT   BINDING      98     98       Quinone (QH). {ECO:0000250}.
FT   BINDING     101    101       Quinone (QH). {ECO:0000250}.
FT   CROSSLNK    284    288       1'-histidyl-3'-tyrosine (His-Tyr).
FT                                {ECO:0000250}.
SQ   SEQUENCE   659 AA;  75028 MW;  23D6FB4B04732D23 CRC64;
     MFGKLTLKAI PVDEPIIMVT YISIILIALF ISFSITYFKK WKYLWYEWFT TVDHKKISIM
     YGILAFIMLF RGFVDAILMR TQQVIASSGN TGFLPPHHYD QIFTAHGVIM IFFVAMPLVI
     GLMNLVVPLQ IGARDVAFPF LNNLSFWLNV SGAILLTLSL GIGEFAQTGW LAYPPLSEVK
     YSPGVGVDYW IWSLQISGVG TTLTGINFLI TILKMRAPGM CFFKMPVFTW AALCTNILIV
     ISFPVLTTTL LLLTLDRCFD FHFFTNNFGG NPMMYVNLIW IWGHPEVYIL VLPVFGVFSE
     VVATFSKKRL FGYVSLVWAT LAITILSFIV WLHHFFTMGA GSNVNAFFGI TTMIIAIPTG
     VKIFNWLFTM YQGRVHMHSS MLWTIGFLIT FSIGGMTGVL LSIPPADFIL HNSLFLVAHF
     HNVIIGGVVF GCFAGINYWF PKLFGFILNE LWGKRAFWFW IIGFFTAFMP LYFLGFMGMT
     RRLSQNIDIE FHFLLSIAAI GAILIGIGIL CQIIQFWVSV RDRHINLDVT GDPWDGRTLE
     WSTSSPAPLY NFAIIPHIKN KDDFWELKKQ KNQVQKKQYS AIHMPKNTGL GIFISFFSLL
     FGFSAVWNII WLSFLSFLVV IISLIFKSID ENTEYTVSVK EIESIENRHL ENVQKAGLK
//
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