CYOB_ECOL6
ID CYOB_ECOL6 Reviewed; 663 AA.
AC P0ABI9; P18401;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1;
DE EC=7.1.1.3 {ECO:0000250|UniProtKB:P0ABI8};
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=c0542;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component
CC of the aerobic respiratory chain of E.coli that predominates when cells
CC are grown at high aeration. Has proton pump activity across the
CC membrane in addition to electron transfer, pumping 2 protons/electron
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out)
CC + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:P0ABI8};
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:132124; 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 the
CC reaction. {ECO:0000250};
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC two D chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in the
CC electron transport chain.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN79020.1; -; Genomic_DNA.
DR RefSeq; WP_000467180.1; NC_004431.1.
DR AlphaFoldDB; P0ABI9; -.
DR SMR; P0ABI9; -.
DR STRING; 199310.c0542; -.
DR EnsemblBacteria; AAN79020; AAN79020; c0542.
DR GeneID; 66671267; -.
DR KEGG; ecc:c0542; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_6; -.
DR OMA; WAMMSIG; -.
DR BioCyc; ECOL199310:C0542-MON; -.
DR Proteomes; UP000001410; 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:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR036927; Cyt_c_oxase-like_su1_sf.
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;
KW Cell inner membrane; Cell membrane; Copper; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..663
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 1"
FT /id="PRO_0000183478"
FT TOPO_DOM 1..16
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 17..35
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 36..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..80
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..95
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..132
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 138..161
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..184
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..215
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250"
FT TOPO_DOM 216..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 225..260
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250"
FT TOPO_DOM 261..270
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 271..307
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250"
FT TOPO_DOM 308..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..326
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000250"
FT TOPO_DOM 327..340
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 341..369
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000250"
FT TOPO_DOM 370..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 378..409
FT /note="Helical; Name=X"
FT /evidence="ECO:0000250"
FT TOPO_DOM 410..412
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 413..445
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000250"
FT TOPO_DOM 446..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 449..477
FT /note="Helical; Name=XII"
FT /evidence="ECO:0000250"
FT TOPO_DOM 478..489
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 490..521
FT /note="Helical; Name=XIII"
FT /evidence="ECO:0000250"
FT TOPO_DOM 522..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 588..606
FT /note="Helical; Name=XIV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 607..613
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 614..632
FT /note="Helical; Name=XV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 633..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Fe(II)-heme o"
FT /ligand_id="ChEBI:CHEBI:60530"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CROSSLNK 284..288
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="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
