CYOC_ECOLI
ID CYOC_ECOLI Reviewed; 204 AA.
AC P0ABJ3; P18402; Q2MBZ6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 3;
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 3;
DE Short=Cytochrome o subunit 3;
DE AltName: Full=Oxidase bo(3) subunit 3;
DE AltName: Full=Ubiquinol oxidase chain C;
DE AltName: Full=Ubiquinol oxidase polypeptide III;
DE AltName: Full=Ubiquinol oxidase subunit 3;
GN Name=cyoC; OrderedLocusNames=b0430, JW0420;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2162835; DOI=10.1016/s0021-9258(19)38574-6;
RA Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.;
RT "The sequence of the cyo operon indicates substantial structural
RT similarities between the cytochrome o ubiquinol oxidase of Escherichia coli
RT and the aa3-type family of cytochrome c oxidases.";
RL J. Biol. Chem. 265:11185-11192(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN UBIQUINOL OXIDATION, FUNCTION IN PROTON ELECTROCHEMICAL
RP GRADIENT GENERATION, AND SUBUNIT.
RX PubMed=6308657; DOI=10.1073/pnas.80.16.4889;
RA Matsushita K., Patel L., Gennis R.B., Kaback H.R.;
RT "Reconstitution of active transport in proteoliposomes containing
RT cytochrome o oxidase and lac carrier protein purified from Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4889-4893(1983).
RN [6]
RP TOPOLOGY.
RX PubMed=2165491; DOI=10.1016/s0021-9258(19)38256-0;
RA Chepuri V., Gennis R.B.;
RT "The use of gene fusions to determine the topology of all of the subunits
RT of the cytochrome o terminal oxidase complex of Escherichia coli.";
RL J. Biol. Chem. 265:12978-12986(1990).
RN [7]
RP TOPOLOGY.
RX PubMed=2168206; DOI=10.1016/0005-2728(90)90231-r;
RA Chepuri V., Lemieux L., Hill J., Alben J.O., Gennis R.B.;
RT "Recent studies of the cytochrome o terminal oxidase complex of Escherichia
RT coli.";
RL Biochim. Biophys. Acta 1018:124-127(1990).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP FUNCTION AS AN OXIDASE, FUNCTION AS A PROTON PUMP, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=19542282; DOI=10.1128/jb.00562-09;
RA Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
RT "Respiration of Escherichia coli can be fully uncoupled via the
RT nonelectrogenic terminal cytochrome bd-II oxidase.";
RL J. Bacteriol. 191:5510-5517(2009).
RN [10]
RP FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=22843529; DOI=10.1128/aem.01507-12;
RA Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.;
RT "Uncoupling of substrate-level phosphorylation in Escherichia coli during
RT glucose-limited growth.";
RL Appl. Environ. Microbiol. 78:6908-6913(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=11017202; DOI=10.1038/82824;
RA Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M.,
RA Puustinen A., Iwata S., Wikstrom M.;
RT "The structure of the ubiquinol oxidase from Escherichia coli and its
RT ubiquinone binding site.";
RL Nat. Struct. Biol. 7:910-917(2000).
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 {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529,
CC ECO:0000269|PubMed:6308657}.
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC two D chains. {ECO:0000269|PubMed:11017202,
CC ECO:0000269|PubMed:6308657}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Increased reduction of the ubiquinone pool (in
CC aerobically grown minimal medium with glucose).
CC {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; J05492; AAA23633.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40186.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73533.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76210.1; -; Genomic_DNA.
DR PIR; C42226; C42226.
DR RefSeq; NP_414964.1; NC_000913.3.
DR RefSeq; WP_000179819.1; NZ_STEB01000007.1.
DR PDB; 1FFT; X-ray; 3.50 A; C/H=25-204.
DR PDB; 6WTI; EM; 2.38 A; C=1-204.
DR PDB; 7CUB; EM; 2.55 A; C=1-204.
DR PDB; 7CUQ; EM; 2.64 A; C=1-204.
DR PDB; 7CUW; EM; 2.63 A; C=1-204.
DR PDBsum; 1FFT; -.
DR PDBsum; 6WTI; -.
DR PDBsum; 7CUB; -.
DR PDBsum; 7CUQ; -.
DR PDBsum; 7CUW; -.
DR AlphaFoldDB; P0ABJ3; -.
DR SMR; P0ABJ3; -.
DR BioGRID; 4261578; 211.
DR ComplexPortal; CPX-2102; Cytochrome bo3 ubiquinol oxidase complex.
DR DIP; DIP-47944N; -.
DR IntAct; P0ABJ3; 1.
DR STRING; 511145.b0430; -.
DR TCDB; 3.D.4.5.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P0ABJ3; -.
DR PRIDE; P0ABJ3; -.
DR EnsemblBacteria; AAC73533; AAC73533; b0430.
DR EnsemblBacteria; BAE76210; BAE76210; BAE76210.
DR GeneID; 66671268; -.
DR GeneID; 946897; -.
DR KEGG; ecj:JW0420; -.
DR KEGG; eco:b0430; -.
DR PATRIC; fig|1411691.4.peg.1847; -.
DR EchoBASE; EB0177; -.
DR eggNOG; COG1845; Bacteria.
DR HOGENOM; CLU_044071_3_0_6; -.
DR InParanoid; P0ABJ3; -.
DR OMA; SIYWWGS; -.
DR PhylomeDB; P0ABJ3; -.
DR BioCyc; EcoCyc:CYOC-MON; -.
DR BioCyc; MetaCyc:CYOC-MON; -.
DR BRENDA; 7.1.1.3; 2026.
DR EvolutionaryTrace; P0ABJ3; -.
DR PRO; PR:P0ABJ3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IDA:EcoCyc.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0015990; P:electron transport coupled proton transport; IDA:ComplexPortal.
DR CDD; cd02863; Ubiquinol_oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR InterPro; IPR014206; Cyt_c_ubiqinol_oxidase_su3.
DR InterPro; IPR033946; Ubiquinol_oxase_su3_dom.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR TIGRFAMs; TIGR02842; CyoC; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Electron transport;
KW Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..204
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 3"
FT /id="PRO_0000183893"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 51..66
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 86..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 121..142
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 162..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 204
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT HELIX 21..49
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 66..91
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 95..124
FT /evidence="ECO:0007829|PDB:6WTI"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 134..167
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 171..197
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:6WTI"
SQ SEQUENCE 204 AA; 22623 MW; F1D6ABF9EB6CB5AD CRC64;
MATDTLTHAT AHAHEHGHHD AGGTKIFGFW IYLMSDCILF SILFATYAVL VNGTAGGPTG
KDIFELPFVL VETFLLLFSS ITYGMAAIAM YKNNKSQVIS WLALTWLFGA GFIGMEIYEF
HHLIVNGMGP DRSGFLSAFF ALVGTHGLHV TSGLIWMAVL MVQIARRGLT STNRTRIMCL
SLFWHFLDVV WICVFTVVYL MGAM
