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Database: UniProt
Entry: P0ABJ1
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Original site: P0ABJ1 
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   29-OCT-2014, entry version 86.
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; 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 277:1453-1462(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   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   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   COFACTOR, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / KL251/ORF4;
RX   PubMed=6365921;
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
RT   the early exponential phase of aerobic growth.";
RL   J. Biol. Chem. 259:3368-3374(1984).
RN   [10]
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   [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
RT   Escherichia 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
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   [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
RT   quinol 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
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   -!- ENZYME 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
CC       uM, 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
CC       and two D chains. {ECO:0000269|PubMed:11017202,
CC       ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:6308657}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:6365921}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:16079137,
CC       ECO:0000269|PubMed:6365921}.
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 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; 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   DisProt; DP00089; -.
DR   ProteinModelPortal; P0ABJ1; -.
DR   SMR; P0ABJ1; 27-283.
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   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   InParanoid; P0ABJ1; -.
DR   KO; K02297; -.
DR   OMA; KIEAVVW; -.
DR   OrthoDB; EOG6PS5TJ; -.
DR   PhylomeDB; P0ABJ1; -.
DR   BioCyc; EcoCyc:CYOA-MONOMER; -.
DR   BioCyc; ECOL316407:JW0422-MONOMER; -.
DR   BioCyc; MetaCyc:CYOA-MONOMER; -.
DR   EvolutionaryTrace; P0ABJ1; -.
DR   PRO; PR:P0ABJ1; -.
DR   Genevestigator; P0ABJ1; -.
DR   GO; GO:0009319; C:cytochrome o ubiquinol oxidase complex; IDA:EcoCyc.
DR   GO; GO:0005887; C:integral component of 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   GO; GO:1902600; P:hydrogen ion transmembrane transport; IDA:GOC.
DR   GO; GO:0055085; P:transmembrane transport; IDA:GOC.
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; 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; 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       {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   CHAIN        25    315       Cytochrome bo(3) ubiquinol oxidase
FT                                subunit 2.
FT                                /FTId=PRO_0000006071.
FT   TOPO_DOM     25     50       Periplasmic. {ECO:0000305}.
FT   TRANSMEM     51     68       Helical. {ECO:0000305}.
FT   TOPO_DOM     69     92       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM     93    111       Helical. {ECO:0000305}.
FT   TOPO_DOM    112    315       Periplasmic. {ECO:0000305}.
FT   LIPID        25     25       N-palmitoyl cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   LIPID        25     25       S-diacylglycerol cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
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
//
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