CYOA_ECOLI
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 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 2;
DE AltName: Full=Cytochrome b562-o complex subunit II;
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 2;
DE Short=Cytochrome o subunit 2;
DE AltName: Full=Oxidase bo(3) subunit 2;
DE AltName: Full=Ubiquinol oxidase chain B;
DE AltName: Full=Ubiquinol oxidase polypeptide II;
DE AltName: Full=Ubiquinol oxidase subunit 2;
DE Flags: Precursor;
GN Name=cyoA; OrderedLocusNames=b0432, JW0422;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=2162837; DOI=10.1016/s0021-9258(19)38576-x;
RA Minagawa J., Nakamura H., Yamato I., Mogi T., Anraku Y.;
RT "Transcriptional regulation of the cytochrome b562-o complex in Escherichia
RT coli. Gene expression and molecular characterization of 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-type
RT oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase
RT with high specific activity.";
RL Biochemistry 31:6917-6924(1992).
RN [8]
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 [9]
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / KL251/ORF4;
RX PubMed=6365921; DOI=10.1016/s0021-9258(17)43304-7;
RA Kita K., Konishi K., Anraku Y.;
RT "Terminal oxidases of Escherichia coli aerobic respiratory chain. I.
RT Purification and properties of cytochrome b562-o complex from cells in the
RT early exponential phase of aerobic growth.";
RL J. Biol. Chem. 259:3368-3374(1984).
RN [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 quinol
RT oxidase complex with an engineered dinuclear copper center.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11955-11959(1995).
RN [17]
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 -!- ACTIVITY REGULATION: Competitively inhibited by piericidin A, non-
CC competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide,
CC NaN(3) and KCN; 50% inhibition occurs at 2 uM, 2 uM, 15 mM and 10 uM,
CC respectively. Inhibited by Zn(2+) and Cd(2+).
CC {ECO:0000269|PubMed:6365921}.
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:16079137, ECO:0000269|PubMed:6308657}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:6365921}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:6365921}.
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 2 family.
CC {ECO:0000305}.
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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_000913.3.
DR RefSeq; WP_001239436.1; NZ_SSZK01000009.1.
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 PDB; 6WTI; EM; 2.38 A; B=1-315.
DR PDB; 7CUB; EM; 2.55 A; B=25-315.
DR PDB; 7CUQ; EM; 2.64 A; B=25-315.
DR PDB; 7CUW; EM; 2.63 A; B=25-315.
DR PDBsum; 1CYW; -.
DR PDBsum; 1CYX; -.
DR PDBsum; 1FFT; -.
DR PDBsum; 6WTI; -.
DR PDBsum; 7CUB; -.
DR PDBsum; 7CUQ; -.
DR PDBsum; 7CUW; -.
DR AlphaFoldDB; P0ABJ1; -.
DR SMR; P0ABJ1; -.
DR BioGRID; 4259512; 300.
DR ComplexPortal; CPX-2102; Cytochrome bo3 ubiquinol oxidase complex.
DR DIP; DIP-47942N; -.
DR IntAct; P0ABJ1; 23.
DR STRING; 511145.b0432; -.
DR TCDB; 3.D.4.5.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR jPOST; P0ABJ1; -.
DR PaxDb; P0ABJ1; -.
DR PRIDE; P0ABJ1; -.
DR EnsemblBacteria; AAC73535; AAC73535; b0432.
DR EnsemblBacteria; BAE76212; BAE76212; BAE76212.
DR GeneID; 67416493; -.
DR GeneID; 945080; -.
DR KEGG; ecj:JW0422; -.
DR KEGG; eco:b0432; -.
DR PATRIC; fig|1411691.4.peg.1845; -.
DR EchoBASE; EB0175; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_6_1_6; -.
DR InParanoid; P0ABJ1; -.
DR OMA; TAMNSFF; -.
DR PhylomeDB; P0ABJ1; -.
DR BioCyc; EcoCyc:CYOA-MON; -.
DR BioCyc; MetaCyc:CYOA-MON; -.
DR BRENDA; 7.1.1.3; 2026.
DR EvolutionaryTrace; P0ABJ1; -.
DR PRO; PR:P0ABJ1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
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:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IDA:ComplexPortal.
DR CDD; cd04212; CuRO_UO_II; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR010514; COX_ARM.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034227; CuRO_UO_II.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR InterPro; IPR006333; Cyt_o_ubiquinol_oxidase_su2.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF06481; COX_ARM; 1.
DR PIRSF; PIRSF000292; Ubi_od_II; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 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;
KW Direct protein sequencing; Electron transport; Lipoprotein; Membrane;
KW Oxidoreductase; Palmitate; Reference proteome; Respiratory chain; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..315
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 2"
FT /id="PRO_0000006071"
FT TOPO_DOM 25..50
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 69..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 112..315
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT REGION 288..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 35..68
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7CUB"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6WTI"
FT HELIX 86..113
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1CYX"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1CYX"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1CYX"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6WTI"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1CYX"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7CUB"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:1CYX"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1CYX"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1CYX"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1CYX"
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
