(data stored in ACNUC7421 zone)

SWISSPROT: CYOB_ECO57

ID   CYOB_ECO57              Reviewed;         663 AA.
AC   P0ABJ0; P18401;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   05-JUL-2017, entry version 92.
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 chain A;
DE   AltName: Full=Ubiquinol oxidase polypeptide I;
DE   AltName: Full=Ubiquinol oxidase subunit 1;
GN   Name=cyoB; OrderedLocusNames=Z0534, ECs0485;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC       Note=Binds 1 copper B ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 low-spin heme b per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme o; Xref=ChEBI:CHEBI:24480; Evidence={ECO:0000250};
CC       Note=Binds 1 high-spin heme o per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=a quinone; Xref=ChEBI:CHEBI:36141; Evidence={ECO:0000250};
CC       Note=Binds 1 high-affinity quinone that appears to function as a
CC       tightly bound cofactor (QH), forming a semiquinone intermediate in
CC       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 inner membrane {ECO:0000250}; Multi-
CC       pass 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}.
DR   EMBL; AE005174; AAG54781.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33908.1; -; Genomic_DNA.
DR   PIR; A85540; A85540.
DR   PIR; E90689; E90689.
DR   RefSeq; NP_308512.1; NC_002695.1.
DR   RefSeq; WP_000467180.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; P0ABJ0; -.
DR   SMR; P0ABJ0; -.
DR   STRING; 155864.Z0534; -.
DR   EnsemblBacteria; AAG54781; AAG54781; Z0534.
DR   EnsemblBacteria; BAB33908; BAB33908; BAB33908.
DR   GeneID; 914587; -.
DR   KEGG; ece:Z0534; -.
DR   KEGG; ecs:ECs0485; -.
DR   PATRIC; fig|386585.9.peg.586; -.
DR   eggNOG; ENOG4105BZ9; Bacteria.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085275; -.
DR   KO; K02298; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
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;
DR   PRODOM; P0ABJ0.
DR   SWISS-2DPAGE; P0ABJ0.
KW   Cell inner membrane; Cell membrane; Complete proteome; Copper;
KW   Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
KW   Membrane; Metal-binding; Oxidoreductase; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    663       Cytochrome bo(3) ubiquinol oxidase
FT                                subunit 1.
FT                                /FTId=PRO_0000183477.
FT   TOPO_DOM      1     16       Periplasmic. {ECO:0000250}.
FT   TRANSMEM     17     35       Helical; Name=I. {ECO:0000250}.
FT   TOPO_DOM     36     52       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     53     80       Helical; Name=II. {ECO:0000250}.
FT   TOPO_DOM     81     95       Periplasmic. {ECO:0000250}.
FT   TRANSMEM     96    132       Helical; Name=III. {ECO:0000250}.
FT   TOPO_DOM    133    137       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    138    161       Helical; Name=IV. {ECO:0000250}.
FT   TOPO_DOM    162    184       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    185    215       Helical; Name=V. {ECO:0000250}.
FT   TOPO_DOM    216    224       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    225    260       Helical; Name=VI. {ECO:0000250}.
FT   TOPO_DOM    261    270       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    271    307       Helical; Name=VII. {ECO:0000250}.
FT   TOPO_DOM    308    311       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    312    326       Helical; Name=VIII. {ECO:0000250}.
FT   TOPO_DOM    327    340       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    341    369       Helical; Name=IX. {ECO:0000250}.
FT   TOPO_DOM    370    377       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    378    409       Helical; Name=X. {ECO:0000250}.
FT   TOPO_DOM    410    412       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    413    445       Helical; Name=XI. {ECO:0000250}.
FT   TOPO_DOM    446    448       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    449    477       Helical; Name=XII. {ECO:0000250}.
FT   TOPO_DOM    478    489       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    490    521       Helical; Name=XIII. {ECO:0000250}.
FT   TOPO_DOM    522    587       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    588    606       Helical; Name=XIV. {ECO:0000250}.
FT   TOPO_DOM    607    613       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    614    632       Helical; Name=XV. {ECO:0000250}.
FT   TOPO_DOM    633    663       Cytoplasmic. {ECO:0000250}.
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   663 AA;  74368 MW;  17357B8D44C7CF84 CRC64;
     MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT SVDHKRLGIM
     YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI
     GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNVSL GVGEFAQTGW LAYPPLSGIE
     YSPGVGVDYW IWSLQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII
     ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
     IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG
     VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF
     HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYALGFMGMT
     RRLSQQIDPQ FHTMLMIAAS GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE
     WATSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST
     IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH FDEITKAGLK
     NGN
//

If you have problems or comments...

PBIL Back to PBIL home page