ID CYOA_ECOLI Reviewed; 315 AA.
AC P0ABJ1; P18400; Q2MBZ4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 01-MAY-2013, entry version 75.
DE RecName: Full=Ubiquinol oxidase subunit 2;
DE EC=1.10.3.-;
DE AltName: Full=Cytochrome o subunit 2;
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 2;
DE Short=Ubiquinol oxidase chain B;
DE AltName: Full=Oxidase BO(3) subunit 2;
DE AltName: Full=Ubiquinol oxidase polypeptide II;
DE Flags: Precursor;
GN Name=cyoA; OrderedLocusNames=b0432, JW0422;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
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 277:1453-1474(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=2162837;
RA Minagawa J., Nakamura H., Yamato I., Mogi T., Anraku Y.;
RT "Transcriptional regulation of the cytochrome b562-o complex in
RT Escherichia coli. Gene expression and molecular characterization of
RT the promoter.";
RL J. Biol. Chem. 265:11198-11203(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RX PubMed=8231804; DOI=10.1111/j.1365-2958.1993.tb01731.x;
RA Lindquist S., Weston-Hafer K., Schmidt H., Pul C., Korfmann G.,
RA Erickson J., Sanders C., Martin H.H., Normark S.;
RT "AmpG, a signal transducer in chromosomal beta-lactamase induction.";
RL Mol. Microbiol. 9:703-715(1993).
RN [7]
RP PROTEIN SEQUENCE OF 153-171.
RX PubMed=1322173; DOI=10.1021/bi00145a008;
RA Minghetti K.C., Goswitz V.C., Gabriel N.E., Hill J.J., Barassi C.A.,
RA Georgiou C.D., Chan S.I., Gennis R.B.;
RT "Modified, large-scale purification of the cytochrome o complex (bo-
RT type oxidase) of Escherichia coli yields a two heme/one copper
RT terminal oxidase with high specific activity.";
RL Biochemistry 31:6917-6924(1992).
RN [8]
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 [9]
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 [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.M506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 111-315.
RX PubMed=8618822; DOI=10.1073/pnas.92.26.11955;
RA Wilmanns M., Lappalainen P., Kelly M., Sauer-Eriksson E., Saraste M.;
RT "Crystal structure of the membrane-exposed domain from a respiratory
RT quinol oxidase complex with an engineered dinuclear copper center.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11955-11959(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
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 o terminal oxidase complex is the component
CC of the aerobic respiratory chain of E.coli that predominates when
CC cells are grown at high aeration.
CC -!- CATALYTIC ACTIVITY: Ubiquinol-8 + O(2) = Ubiquinone-8 + H(2)O.
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains
CC and two D chains.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
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DR EMBL; J05492; AAA23631.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40188.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73535.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76212.1; -; Genomic_DNA.
DR EMBL; M55258; AAA23630.1; -; Genomic_DNA.
DR EMBL; S67816; AAB28885.1; -; Genomic_DNA.
DR PIR; A42226; A42226.
DR RefSeq; NP_414966.1; NC_000913.2.
DR RefSeq; YP_488724.1; NC_007779.1.
DR PDB; 1CYW; X-ray; 2.50 A; A=111-315.
DR PDB; 1CYX; X-ray; 2.30 A; A=111-315.
DR PDB; 1FFT; X-ray; 3.50 A; B/G=1-315.
DR PDBsum; 1CYW; -.
DR PDBsum; 1CYX; -.
DR PDBsum; 1FFT; -.
DR ProteinModelPortal; P0ABJ1; -.
DR SMR; P0ABJ1; 27-283.
DR DIP; DIP-47942N; -.
DR IntAct; P0ABJ1; 20.
DR STRING; 511145.b0432; -.
DR TCDB; 3.D.4.5.1; proton-translocating cytochrome oxidase (COX) superfamily.
DR PaxDb; P0ABJ1; -.
DR PRIDE; P0ABJ1; -.
DR EnsemblBacteria; AAC73535; AAC73535; b0432.
DR EnsemblBacteria; BAE76212; BAE76212; BAE76212.
DR GeneID; 12930518; -.
DR GeneID; 945080; -.
DR KEGG; ecj:Y75_p0420; -.
DR KEGG; eco:b0432; -.
DR PATRIC; 32116015; VBIEscCol129921_0449.
DR EchoBASE; EB0175; -.
DR EcoGene; EG10178; cyoA.
DR eggNOG; COG1622; -.
DR HOGENOM; HOG000084157; -.
DR KO; K02297; -.
DR OMA; NKIFGML; -.
DR ProtClustDB; PRK10525; -.
DR BioCyc; EcoCyc:CYOA-MONOMER; -.
DR BioCyc; ECOL316407:JW0422-MONOMER; -.
DR BioCyc; MetaCyc:CYOA-MONOMER; -.
DR EvolutionaryTrace; P0ABJ1; -.
DR Genevestigator; P0ABJ1; -.
DR GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:EcoliWiki.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
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:0048039; F:ubiquinone binding; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IMP:EcoCyc.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR012141; Bo-type_Ubol_Oxase_su_II.
DR InterPro; IPR010514; COX_ARM.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR006333; Cyt_o_ubiquinol_oxidase_su2.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF06481; COX_ARM; 1.
DR PIRSF; PIRSF000292; Ubi_od_II; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR TIGRFAMs; TIGR01433; CyoA; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
KW Direct protein sequencing; Electron transport; Lipoprotein; Membrane;
KW Oxidoreductase; Palmitate; Reference proteome; Respiratory chain;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 315 Ubiquinol oxidase subunit 2.
FT /FTId=PRO_0000006071.
FT TOPO_DOM 25 50 Periplasmic (Probable).
FT TRANSMEM 51 68 Helical; (Probable).
FT TOPO_DOM 69 92 Cytoplasmic (Probable).
FT TRANSMEM 93 111 Helical; (Probable).
FT TOPO_DOM 112 315 Periplasmic (Probable).
FT LIPID 25 25 N-palmitoyl cysteine (Potential).
FT LIPID 25 25 S-diacylglycerol cysteine (Potential).
FT HELIX 37 50
FT TURN 51 56
FT HELIX 57 63
FT TURN 64 71
FT TURN 73 75
FT HELIX 87 91
FT HELIX 94 110
FT STRAND 127 134
FT STRAND 137 142
FT TURN 143 146
FT STRAND 147 156
FT STRAND 161 170
FT STRAND 172 176
FT HELIX 177 179
FT STRAND 181 185
FT STRAND 191 195
FT STRAND 198 207
FT TURN 213 217
FT STRAND 220 227
FT HELIX 228 239
FT HELIX 248 255
FT STRAND 264 267
FT HELIX 273 278
FT TURN 279 281
SQ SEQUENCE 315 AA; 34911 MW; 62EC951183B65724 CRC64;
MRLRKYNKSL GWLSLFAGTV LLSGCNSALL DPKGQIGLEQ RSLILTAFGL MLIVVIPAIL
MAVGFAWKYR ASNKDAKYSP NWSHSNKVEA VVWTVPILII IFLAVLTWKT THALEPSKPL
AHDEKPITIE VVSMDWKWFF IYPEQGIATV NEIAFPANTP VYFKVTSNSV MNSFFIPRLG
SQIYAMAGMQ TRLHLIANEP GTYDGISASY SGPGFSGMKF KAIATPDRAA FDQWVAKAKQ
SPNTMSDMAA FEKLAAPSEY NQVEYFSNVK PDLFADVINK FMAHGKSMDM TQPEGEHSAH
EGMEGMDMSH AESAH
//
