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 18-JAN-2017, entry version 94.
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;
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
RT coli 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.,
RA Mau B., 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
RT MG1655 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;
RA Chepuri V., Gennis R.B.;
RT "The use of gene fusions to determine the topology of all of the
RT subunits of the cytochrome o terminal oxidase complex of Escherichia
RT 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
RT Escherichia 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
RP DISRUPTION 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
RT during 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
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.
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
CC and two D chains. {ECO:0000269|PubMed:11017202,
CC ECO:0000269|PubMed:6308657}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein.
CC -!- DISRUPTION PHENOTYPE: Increased reduction of the ubiquinone pool
CC (in 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}.
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_LN832404.1.
DR PDB; 1FFT; X-ray; 3.50 A; C/H=25-204.
DR PDBsum; 1FFT; -.
DR ProteinModelPortal; P0ABJ3; -.
DR BioGrid; 4261578; 196.
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; 946897; -.
DR KEGG; ecj:JW0420; -.
DR KEGG; eco:b0430; -.
DR PATRIC; 32116011; VBIEscCol129921_0447.
DR EchoBASE; EB0177; -.
DR EcoGene; EG10180; cyoC.
DR eggNOG; ENOG4105CCU; Bacteria.
DR eggNOG; COG1845; LUCA.
DR HOGENOM; HOG000086398; -.
DR InParanoid; P0ABJ3; -.
DR KO; K02299; -.
DR OMA; YTELVKH; -.
DR PhylomeDB; P0ABJ3; -.
DR BioCyc; EcoCyc:CYOC-MONOMER; -.
DR BioCyc; ECOL316407:JW0420-MONOMER; -.
DR BioCyc; MetaCyc:CYOC-MONOMER; -.
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:EcoCyc.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IDA:EcoCyc.
DR GO; GO:0008827; F:cytochrome o ubiquinol oxidase activity; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0015990; P:electron transport coupled proton transport; IDA:EcoCyc.
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; 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; Complete proteome;
KW Electron transport; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 204 Cytochrome bo(3) ubiquinol oxidase
FT subunit 3.
FT /FTId=PRO_0000183893.
FT TOPO_DOM 1 31 Cytoplasmic. {ECO:0000305}.
FT TRANSMEM 32 50 Helical. {ECO:0000305}.
FT TOPO_DOM 51 66 Periplasmic. {ECO:0000305}.
FT TRANSMEM 67 85 Helical. {ECO:0000305}.
FT TOPO_DOM 86 101 Cytoplasmic. {ECO:0000305}.
FT TRANSMEM 102 120 Helical. {ECO:0000305}.
FT TOPO_DOM 121 142 Periplasmic. {ECO:0000305}.
FT TRANSMEM 143 161 Helical. {ECO:0000305}.
FT TOPO_DOM 162 184 Cytoplasmic. {ECO:0000305}.
FT TRANSMEM 185 203 Helical. {ECO:0000305}.
FT TOPO_DOM 204 204 Periplasmic. {ECO:0000305}.
FT HELIX 25 30 {ECO:0000244|PDB:1FFT}.
FT HELIX 33 36 {ECO:0000244|PDB:1FFT}.
FT HELIX 39 47 {ECO:0000244|PDB:1FFT}.
FT TURN 48 53 {ECO:0000244|PDB:1FFT}.
FT HELIX 66 76 {ECO:0000244|PDB:1FFT}.
FT HELIX 77 79 {ECO:0000244|PDB:1FFT}.
FT TURN 80 84 {ECO:0000244|PDB:1FFT}.
FT HELIX 86 88 {ECO:0000244|PDB:1FFT}.
FT TURN 89 92 {ECO:0000244|PDB:1FFT}.
FT HELIX 95 98 {ECO:0000244|PDB:1FFT}.
FT HELIX 100 125 {ECO:0000244|PDB:1FFT}.
FT TURN 135 137 {ECO:0000244|PDB:1FFT}.
FT HELIX 138 146 {ECO:0000244|PDB:1FFT}.
FT HELIX 149 152 {ECO:0000244|PDB:1FFT}.
FT HELIX 155 166 {ECO:0000244|PDB:1FFT}.
FT HELIX 176 194 {ECO:0000244|PDB:1FFT}.
FT HELIX 195 202 {ECO:0000244|PDB:1FFT}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 16 202 ipfam:COX3 [T]
FT MYHIT 1 203 iprf:COX3 [T]
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
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