CUEO_ECOLI
ID CUEO_ECOLI Reviewed; 516 AA.
AC P36649; P75655; Q8KMZ0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Multicopper oxidase CueO {ECO:0000303|PubMed:11222619};
DE Short=MCO {ECO:0000303|PubMed:20088522};
DE EC=1.16.3.- {ECO:0000269|PubMed:15516598, ECO:0000269|PubMed:20088522};
DE AltName: Full=Blue copper oxidase CueO;
DE AltName: Full=Copper efflux oxidase {ECO:0000305};
DE Short=Cu efflux oxidase {ECO:0000303|PubMed:10915804};
DE AltName: Full=Cuprous oxidase {ECO:0000303|PubMed:15516598};
DE Flags: Precursor;
GN Name=cueO {ECO:0000303|PubMed:10915804}; Synonyms=yacK;
GN OrderedLocusNames=b0123, JW0119;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 [4]
RP PROTEIN SEQUENCE OF 29-40.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [6]
RP EXPORT VIA THE TAT-SYSTEM, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-3
RP AND LYS-8.
RX PubMed=10766774; DOI=10.1074/jbc.275.16.11591;
RA Stanley N.R., Palmer T., Berks B.C.;
RT "The twin arginine consensus motif of Tat signal peptides is involved in
RT Sec-independent protein targeting in Escherichia coli.";
RL J. Biol. Chem. 275:11591-11596(2000).
RN [7]
RP NOMENCLATURE, AND INDUCTION BY CUER.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=10915804; DOI=10.1074/jbc.m006508200;
RA Outten F.W., Outten C.E., Hale J.A., O'Halloran T.V.;
RT "Transcriptional activation of an Escherichia coli copper efflux regulon by
RT the chromosomal merR homologue, cueR.";
RL J. Biol. Chem. 275:31024-31029(2000).
RN [8]
RP POSSIBLE FUNCTION IN COPPER TOLERANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=11222619; DOI=10.1128/jb.183.6.2145-2147.2001;
RA Grass G., Rensing C.;
RT "Genes involved in copper homeostasis in Escherichia coli.";
RL J. Bacteriol. 183:2145-2147(2001).
RN [9]
RP FUNCTION IN COPPER TOLERANCE, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11399769; DOI=10.1074/jbc.m104122200;
RA Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
RT "The independent cue and cus systems confer copper tolerance during aerobic
RT and anaerobic growth in Escherichia coli.";
RL J. Biol. Chem. 276:30670-30677(2001).
RN [10]
RP FUNCTION AS FERROXIDASE AND PHENOLOXIDASE, COFACTOR, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=11466290; DOI=10.1128/jb.183.16.4866-4875.2001;
RA Kim C., Lorenz W.W., Hoopes J.T., Dean J.F.D.;
RT "Oxidation of phenolate siderophores by the multicopper oxidase encoded by
RT the Escherichia coli yacK gene.";
RL J. Bacteriol. 183:4866-4875(2001).
RN [11]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 500-CYS-HIS-501.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11527384; DOI=10.1006/bbrc.2001.5474;
RA Grass G., Rensing C.;
RT "CueO is a multi-copper oxidase that confers copper tolerance in
RT Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 286:902-908(2001).
RN [12]
RP FUNCTION IN ENTEROBACTIN OXIDATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15317788; DOI=10.1128/jb.186.17.5826-5833.2004;
RA Grass G., Thakali K., Klebba P.E., Thieme D., Mueller A., Wildner G.F.,
RA Rensing C.;
RT "Linkage between catecholate siderophores and the multicopper oxidase CueO
RT in Escherichia coli.";
RL J. Bacteriol. 186:5826-5833(2004).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF CYS-500.
RX PubMed=15516598; DOI=10.1128/jb.186.22.7815-7817.2004;
RA Singh S.K., Grass G., Rensing C., Montfort W.R.;
RT "Cuprous oxidase activity of CueO from Escherichia coli.";
RL J. Bacteriol. 186:7815-7817(2004).
RN [14]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [15]
RP FUNCTION IN VIVO, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=20088522; DOI=10.1021/ja9091903;
RA Djoko K.Y., Chong L.X., Wedd A.G., Xiao Z.;
RT "Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli
RT support its functional role as a cuprous oxidase.";
RL J. Am. Chem. Soc. 132:2005-2015(2010).
RN [16]
RP FUNCTION, AND DOMAIN.
RX PubMed=25679350; DOI=10.1039/c5mt00001g;
RA Cortes L., Wedd A.G., Xiao Z.;
RT "The functional roles of the three copper sites associated with the
RT methionine-rich insert in the multicopper oxidase CueO from E. coli.";
RL Metallomics 7:776-785(2015).
RN [17]
RP SUBCELLULAR LOCATION, AND EXPORT VIA THE TAT-SYSTEM.
RX PubMed=27129241; DOI=10.1074/jbc.m116.729103;
RA Stolle P., Hou B., Brueser T.;
RT "The Tat substrate CueO is transported in an incomplete folding state.";
RL J. Biol. Chem. 291:13520-13528(2016).
RN [18]
RP BIOTECHNOLOGY.
RX PubMed=33332702; DOI=10.1002/cbic.202000775;
RA Decembrino D., Girhard M., Urlacher V.B.;
RT "Use of copper as a trigger for the in vivo activity of E. coli laccase
RT CueO: a simple tool for biosynthetic purposes.";
RL ChemBioChem 22:1470-1479(2021).
RN [19] {ECO:0007744|PDB:1KV7}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH COPPER, FUNCTION AS A
RP PHENOLOXIDASE, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DOMAIN.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11867755; DOI=10.1073/pnas.052710499;
RA Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T., Tollin G.,
RA Rensing C., Montfort W.R.;
RT "Crystal structure and electron transfer kinetics of CueO, a multicopper
RT oxidase required for copper homeostasis in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2766-2771(2002).
RN [20] {ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-516 IN COMPLEXES WITH COPPER,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, DOMAIN, AND
RP MUTAGENESIS OF MET-355; ASP-360; ASP-439 AND MET-441.
RX PubMed=12794077; DOI=10.1074/jbc.m302963200;
RA Roberts S.A., Wildner G.F., Grass G., Weichsel A., Ambrus A., Rensing C.,
RA Montfort W.R.;
RT "A labile regulatory copper ion lies near the T1 copper site in the
RT multicopper oxidase CueO.";
RL J. Biol. Chem. 278:31958-31963(2003).
RN [21] {ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 29-516 IN COMPLEXES WITH COPPER,
RP COFACTOR, AND MUTAGENESIS OF GLU-106.
RX PubMed=17217912; DOI=10.1016/j.bbrc.2006.12.116;
RA Li X., Wei Z., Zhang M., Peng X., Yu G., Teng M., Gong W.;
RT "Crystal structures of E. coli laccase CueO at different copper
RT concentrations.";
RL Biochem. Biophys. Res. Commun. 354:21-26(2007).
RN [22] {ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW}
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS) OF 29-516 OF METHIONINE-RICH
RP TRUNCATED MUTANT IN COMPLEXES WITH COPPER, FUNCTION, ACTIVITY REGULATION,
RP COFACTOR, AND MUTAGENESIS OF 357-PRO--HIS-406.
RX PubMed=17804014; DOI=10.1016/j.jmb.2007.07.041;
RA Kataoka K., Komori H., Ueki Y., Konno Y., Kamitaka Y., Kurose S.,
RA Tsujimura S., Higuchi Y., Kano K., Seo D., Sakurai T.;
RT "Structure and function of the engineered multicopper oxidase CueO from
RT Escherichia coli--deletion of the methionine-rich helical region covering
RT the substrate-binding site.";
RL J. Mol. Biol. 373:141-152(2007).
RN [23] {ECO:0007744|PDB:3NSC, ECO:0007744|PDB:3NSD, ECO:0007744|PDB:3NSF, ECO:0007744|PDB:3NSY, ECO:0007744|PDB:3NT0, ECO:0007744|PDB:3OD3}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 29-516 OF APOENZYME; WILD-TYPE
RP AND MUTANTS IN COMPLEXES WITH COPPER AND SILVER, ACTIVITY REGULATION,
RP COFACTOR, AND DOMAIN.
RX PubMed=21903583; DOI=10.1074/jbc.m111.293589;
RA Singh S.K., Roberts S.A., McDevitt S.F., Weichsel A., Wildner G.F.,
RA Grass G.B., Rensing C., Montfort W.R.;
RT "Crystal structures of multicopper oxidase CueO bound to copper(I) and
RT silver(I): functional role of a methionine-rich sequence.";
RL J. Biol. Chem. 286:37849-37857(2011).
RN [24] {ECO:0007744|PDB:4E9Q, ECO:0007744|PDB:4E9R, ECO:0007744|PDB:4E9S, ECO:0007744|PDB:4E9T, ECO:0007744|PDB:4NER}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-516 IN COMPLEXES WITH COPPER.
RX PubMed=24598746; DOI=10.1107/s1399004713033051;
RA Komori H., Sugiyama R., Kataoka K., Miyazaki K., Higuchi Y., Sakurai T.;
RT "New insights into the catalytic active-site structure of multicopper
RT oxidases.";
RL Acta Crystallogr. D 70:772-779(2014).
RN [25] {ECO:0007744|PDB:4EF3}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-516 IN COMPLEX WITH COPPER.
RX PubMed=27380373; DOI=10.1107/s2053230x16009237;
RA Komori H., Kataoka K., Tanaka S., Matsuda N., Higuchi Y., Sakurai T.;
RT "Exogenous acetate ion reaches the type II copper centre in CueO through
RT the water-excretion channel and potentially affects the enzymatic
RT activity.";
RL Acta Crystallogr. F Struct. Biol. Commun. 72:558-563(2016).
RN [26] {ECO:0007744|PDB:5YS1, ECO:0007744|PDB:5YS5}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF MUTANT LYS-304 IN COMPLEXES WITH
RP COPPER, AND MUTAGENESIS OF GLY-304.
RX PubMed=30250139; DOI=10.1038/s41598-018-32446-7;
RA Wang H., Liu X., Zhao J., Yue Q., Yan Y., Gao Z., Dong Y., Zhang Z.,
RA Fan Y., Tian J., Wu N., Gong Y.;
RT "Crystal structures of multicopper oxidase CueO G304K mutant: structural
RT basis of the increased laccase activity.";
RL Sci. Rep. 8:14252-14252(2018).
RN [27] {ECO:0007744|PDB:6IM7, ECO:0007744|PDB:6IM8, ECO:0007744|PDB:6IM9}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 29-516, AND BIOTECHNOLOGY.
RX PubMed=30770473; DOI=10.1074/jbc.ra118.007141;
RA Sana B., Chee S.M.Q., Wongsantichon J., Raghavan S., Robinson R.C.,
RA Ghadessy F.J.;
RT "Development and structural characterization of an engineered multi-copper
RT oxidase reporter of protein-protein interactions.";
RL J. Biol. Chem. 294:7002-7012(2019).
CC -!- FUNCTION: Multicopper oxidase involved in copper homeostasis and copper
CC tolerance under aerobic conditions (PubMed:11222619, PubMed:11399769,
CC PubMed:11527384, PubMed:15516598). Is responsible for the oxidation of
CC Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing
CC Cu(+) from entering the cytoplasm (PubMed:15516598, PubMed:20088522,
CC PubMed:25679350). Probably primarily functions as a cuprous oxidase in
CC vivo (PubMed:20088522). {ECO:0000269|PubMed:11222619,
CC ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:11527384,
CC ECO:0000269|PubMed:15516598, ECO:0000269|PubMed:20088522,
CC ECO:0000269|PubMed:25679350}.
CC -!- FUNCTION: In vitro, in the presence of excess copper ions, exhibits
CC ferroxidase and phenoloxidase activities (PubMed:11466290,
CC PubMed:11527384, PubMed:11867755, PubMed:15317788, PubMed:15516598,
CC PubMed:17804014, PubMed:25679350). Fe(2+) is an excellent substrate in
CC the presence of excess Cu(2+), but is inactive in the absence of Cu(2+)
CC (PubMed:15516598, PubMed:17804014). Oxidizes the phenolate iron
CC siderophores enterobactin, 2,3-dihydroxybenzoate (2,3-DHB) and 3-
CC hydroxyanthranilate (3-HAA) (PubMed:11466290, PubMed:15317788).
CC Oxidation and thus inactivation of enterobactin could protect cells
CC from the interaction of enterobactin with copper and play a central
CC role as an interface between copper detoxification and iron homeostasis
CC (PubMed:11466290, PubMed:15317788). Also oxidizes a variety of phenolic
CC model substrates, including 2,2'-azinobis(3-ethylbenzthiazolinesulfonic
CC acid) (ABTS), p-phenylenediamine (pPD), 2,6-dimethoxyphenol (2,6-DMP)
CC and 3,4-dihydroxybenzoic acid (3,4-DHB) (PubMed:11466290,
CC PubMed:11527384, PubMed:17804014, PubMed:25679350).
CC {ECO:0000269|PubMed:11466290, ECO:0000269|PubMed:11527384,
CC ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:15317788,
CC ECO:0000269|PubMed:15516598, ECO:0000269|PubMed:17804014,
CC ECO:0000269|PubMed:25679350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Cu(+) + 4 H(+) + O2 = 4 Cu(2+) + 2 H2O;
CC Xref=Rhea:RHEA:30083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552;
CC Evidence={ECO:0000269|PubMed:15516598, ECO:0000269|PubMed:20088522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30084;
CC Evidence={ECO:0000269|PubMed:15516598, ECO:0000269|PubMed:20088522};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:11466290, ECO:0000269|PubMed:11527384,
CC ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:20088522};
CC Note=Binds 4 Cu cations per monomer (PubMed:11527384, PubMed:11867755,
CC PubMed:12794077, PubMed:17217912, PubMed:17804014, PubMed:21903583,
CC PubMed:24598746, PubMed:27380373, PubMed:30250139). Contains a
CC mononuclear type 1 (T1) or 'blue' copper site, and a trinuclear copper
CC center consisting of one type 2 (T2) or 'normal' copper site, and two
CC type 3 (T3) or 'binuclear' copper sites (PubMed:11867755).
CC {ECO:0000269|PubMed:11527384, ECO:0000269|PubMed:11867755,
CC ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
CC ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
CC ECO:0000269|PubMed:24598746, ECO:0000269|PubMed:27380373,
CC ECO:0000269|PubMed:30250139};
CC -!- ACTIVITY REGULATION: Ferroxidase and phenoloxidase activities are
CC enhanced considerably in the presence of excess copper ions
CC (PubMed:11466290, PubMed:11527384, PubMed:11867755, PubMed:15516598,
CC PubMed:17804014). A labile regulatory copper ion near the T1 copper
CC site is important for the copper associated activation of enzyme
CC activity (PubMed:12794077). Ag(+) acts as a potent inhibitor of oxidase
CC activity by binding at Cu(+) binding sites, blocking Cu(+) substrate
CC binding and oxidation (PubMed:21903583). pPD oxidase activity is
CC strongly inhibited by sodium azide, an inhibitor of the electron
CC transfer (PubMed:11527384). {ECO:0000269|PubMed:11466290,
CC ECO:0000269|PubMed:11527384, ECO:0000269|PubMed:11867755,
CC ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:15516598,
CC ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=165 uM for Cu(+) (at pH 5.0, in the absence of added Cu(2+))
CC {ECO:0000269|PubMed:15516598};
CC KM=169 uM for Cu(+) (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:15516598};
CC KM=90 uM for Cu(+) (at pH 7.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:15516598};
CC KM=129 uM for Fe(2+) (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:15516598};
CC KM=70 uM for Fe(2+) (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=40 uM for enterobactin (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=1.5 uM for ferric enterobactin (at pH 6.5, in the presence of 0.5
CC mM Cu(2+)) {ECO:0000269|PubMed:15317788};
CC KM=290 uM for 2,3-DHB (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=690 uM for 3-HAA (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=2500 uM for ABTS (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=3200 uM for pPD (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=2120 uM for 2,6-DMP (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC KM=70.5 uM for 2,6-DMP (at pH 6.5, in the presence of 250 uM Cu(2+))
CC {ECO:0000269|PubMed:11867755};
CC KM=430 uM for 3,4-DHB (at pH 5.0, in the presence of 1 mM Cu(2+))
CC {ECO:0000269|PubMed:11466290};
CC Vmax=41.0 umol/min/mg enzyme with Fe(2+) as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=9.70 umol/min/mg enzyme with enterobactin as substrate (at pH
CC 5.0, in the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=3.80 umol/min/mg enzyme with 2,3-DHB as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=63.90 umol/min/mg enzyme with 3-HAA as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=72.10 umol/min/mg enzyme with ABTS as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=95.90 umol/min/mg enzyme with pPD as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=91.70 umol/min/mg enzyme with 2,6-DMP as substrate (at pH 5.0,
CC in the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Vmax=7.20 umol/min/mg enzyme with 3,4-DHB as substrate (at pH 5.0, in
CC the presence of 1 mM Cu(2+)) {ECO:0000269|PubMed:11466290};
CC Note=kcat is 914 min(-1) with Cu(+) as substrate (at pH 5.0, in the
CC absence of added Cu(2+)) (PubMed:15516598). kcat is 651 min(-1) with
CC Cu(+) as substrate (at pH 5.0, in the presence of 1 mM Cu(2+))
CC (PubMed:15516598). kcat is 57 min(-1) with Cu(+) as substrate (at pH
CC 7.0, in the presence of 1 mM Cu(2+)) (PubMed:15516598). kcat is 215
CC min(-1) with Fe(2+) as substrate (at pH 5.0, in the presence of 1 mM
CC Cu(2+)) (PubMed:15516598). kcat is 120 sec(-1) with 2,6-DMP as
CC substrate (PubMed:11867755). {ECO:0000269|PubMed:11867755,
CC ECO:0000269|PubMed:15516598};
CC pH dependence:
CC Optimum pH is 6.5 with 2,6-DMP as substrate (PubMed:11867755). The pH
CC dependence of the reaction as monitored by oxygen consumption shows a
CC broad activity peak between pH 5 and 6 and a second activity peak at
CC pH 8 (PubMed:12794077). {ECO:0000269|PubMed:11867755,
CC ECO:0000269|PubMed:12794077};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius with 2,6-DMP as substrate.
CC {ECO:0000269|PubMed:11867755};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11867755,
CC ECO:0000305|PubMed:11527384}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10766774,
CC ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:11527384,
CC ECO:0000269|PubMed:27129241}. Note=Exported via the Tat pathway
CC (PubMed:10766774, PubMed:17218314, PubMed:27129241). Cytoplasmic CueO
CC does not contain copper, even under copper stress conditions, and is
CC transported as an apo-protein to the periplasm. Periplasmic CueO is
CC readily activated by the addition of copper ions in vitro or under
CC copper stress conditions in vivo (PubMed:27129241). Can also be
CC exported by the Sec system (PubMed:17218314).
CC {ECO:0000269|PubMed:10766774, ECO:0000269|PubMed:17218314,
CC ECO:0000269|PubMed:27129241}.
CC -!- INDUCTION: By CueR, in response to increasing copper concentrations.
CC {ECO:0000269|PubMed:10915804}.
CC -!- DOMAIN: Contains a methionine-rich region, which includes a helix that
CC covers the entrance to the type 1 (T1) copper site and blocks access to
CC the T1 site in the absence of excess copper (PubMed:11867755,
CC PubMed:21903583). This methionine-rich insert is involved in the
CC binding and oxidation of Cu(+) (PubMed:21903583). It also binds
CC additional copper ions, which are important for the copper-associated
CC regulation of activity (PubMed:11867755, PubMed:12794077,
CC PubMed:21903583). The methionine-rich region provides at least three
CC additional Cu(+) binding sites: Cu5 (sCu), Cu6 and Cu7, which play
CC related but distinct roles in CueO oxidase activities
CC (PubMed:25679350). The internal Cu5 site functions as an electron-
CC transfer mediator connecting surface-exposed sites Cu6 and Cu7 to site
CC T1. Both Cu6 and Cu7 are probable substrate oxidation sites on the
CC protein surface (PubMed:25679350). {ECO:0000269|PubMed:11867755,
CC ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:21903583,
CC ECO:0000269|PubMed:25679350}.
CC -!- PTM: Exported by the Tat system (PubMed:10766774, PubMed:17218314,
CC PubMed:27129241). The position of the signal peptide cleavage has been
CC experimentally proven (PubMed:9298646). {ECO:0000269|PubMed:10766774,
CC ECO:0000269|PubMed:17218314, ECO:0000269|PubMed:27129241,
CC ECO:0000269|PubMed:9298646}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant is slightly more copper
CC sensitive on complex medium than wild-type strain under aerobic
CC conditions (PubMed:11222619, PubMed:11399769). Deletion of the gene
CC does not affect copper sensitivity under anaerobic growth conditions
CC (PubMed:11399769). Deletion of the gene leads to elevated biosynthesis
CC of enterobactin under conditions of iron scarcity when copper is
CC present (PubMed:15317788). {ECO:0000269|PubMed:11222619,
CC ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:15317788}.
CC -!- BIOTECHNOLOGY: Triggering CueO activity at need by the addition of
CC copper salts with minor toxic effects on E.coli cells could be used as
CC a simple tool for biosynthetic purposes (PubMed:33332702). The protein
CC was also identified as robust host protein for use in biosensing and
CC drug-screening applications (PubMed:30770473).
CC {ECO:0000269|PubMed:30770473, ECO:0000269|PubMed:33332702}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U00096; AAC73234.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96698.2; -; Genomic_DNA.
DR PIR; C64735; C64735.
DR RefSeq; NP_414665.1; NC_000913.3.
DR RefSeq; WP_001189647.1; NZ_STEB01000010.1.
DR PDB; 1KV7; X-ray; 1.40 A; A=29-516.
DR PDB; 1N68; X-ray; 1.70 A; A=29-516.
DR PDB; 1PF3; X-ray; 1.50 A; A=29-516.
DR PDB; 2FQD; X-ray; 2.40 A; A=29-516.
DR PDB; 2FQE; X-ray; 1.92 A; A=29-516.
DR PDB; 2FQF; X-ray; 2.00 A; A=29-516.
DR PDB; 2FQG; X-ray; 2.30 A; A=29-516.
DR PDB; 2YXV; X-ray; 1.81 A; A/B=29-516.
DR PDB; 2YXW; X-ray; 1.50 A; A/B=29-516.
DR PDB; 3NSC; X-ray; 1.50 A; A=29-516.
DR PDB; 3NSD; X-ray; 2.00 A; A=29-516.
DR PDB; 3NSF; X-ray; 2.00 A; A=29-516.
DR PDB; 3NSY; X-ray; 2.10 A; A=29-516.
DR PDB; 3NT0; X-ray; 1.80 A; A=29-516.
DR PDB; 3OD3; X-ray; 1.10 A; A=29-516.
DR PDB; 3PAU; X-ray; 2.00 A; A=29-516.
DR PDB; 3PAV; X-ray; 1.45 A; A=29-516.
DR PDB; 3QQX; X-ray; 1.50 A; A=29-516.
DR PDB; 3UAA; X-ray; 1.70 A; A=29-516.
DR PDB; 3UAB; X-ray; 1.30 A; A=29-516.
DR PDB; 3UAC; X-ray; 1.30 A; A=29-516.
DR PDB; 3UAD; X-ray; 1.10 A; A=29-516.
DR PDB; 3UAE; X-ray; 1.30 A; A=29-516.
DR PDB; 4E9Q; X-ray; 1.30 A; A=29-516.
DR PDB; 4E9R; X-ray; 1.30 A; A=29-516.
DR PDB; 4E9S; X-ray; 1.06 A; A=29-516.
DR PDB; 4E9T; X-ray; 1.30 A; A=29-516.
DR PDB; 4EF3; X-ray; 1.90 A; A=29-516.
DR PDB; 4HAK; X-ray; 1.40 A; A=29-516.
DR PDB; 4HAL; X-ray; 1.40 A; A=29-516.
DR PDB; 4NER; X-ray; 1.60 A; A=29-516.
DR PDB; 5B7E; X-ray; 1.42 A; A=1-516.
DR PDB; 5B7F; X-ray; 1.45 A; A=29-516.
DR PDB; 5B7M; X-ray; 1.80 A; A/B/C=29-516.
DR PDB; 5YS1; X-ray; 1.49 A; A=1-516.
DR PDB; 5YS5; X-ray; 2.20 A; A=1-516.
DR PDB; 6IM7; X-ray; 1.97 A; A=29-516.
DR PDB; 6IM8; X-ray; 1.80 A; A=29-516.
DR PDB; 6IM9; X-ray; 3.30 A; A=29-516.
DR PDBsum; 1KV7; -.
DR PDBsum; 1N68; -.
DR PDBsum; 1PF3; -.
DR PDBsum; 2FQD; -.
DR PDBsum; 2FQE; -.
DR PDBsum; 2FQF; -.
DR PDBsum; 2FQG; -.
DR PDBsum; 2YXV; -.
DR PDBsum; 2YXW; -.
DR PDBsum; 3NSC; -.
DR PDBsum; 3NSD; -.
DR PDBsum; 3NSF; -.
DR PDBsum; 3NSY; -.
DR PDBsum; 3NT0; -.
DR PDBsum; 3OD3; -.
DR PDBsum; 3PAU; -.
DR PDBsum; 3PAV; -.
DR PDBsum; 3QQX; -.
DR PDBsum; 3UAA; -.
DR PDBsum; 3UAB; -.
DR PDBsum; 3UAC; -.
DR PDBsum; 3UAD; -.
DR PDBsum; 3UAE; -.
DR PDBsum; 4E9Q; -.
DR PDBsum; 4E9R; -.
DR PDBsum; 4E9S; -.
DR PDBsum; 4E9T; -.
DR PDBsum; 4EF3; -.
DR PDBsum; 4HAK; -.
DR PDBsum; 4HAL; -.
DR PDBsum; 4NER; -.
DR PDBsum; 5B7E; -.
DR PDBsum; 5B7F; -.
DR PDBsum; 5B7M; -.
DR PDBsum; 5YS1; -.
DR PDBsum; 5YS5; -.
DR PDBsum; 6IM7; -.
DR PDBsum; 6IM8; -.
DR PDBsum; 6IM9; -.
DR AlphaFoldDB; P36649; -.
DR SMR; P36649; -.
DR BioGRID; 4261957; 17.
DR DIP; DIP-11178N; -.
DR IntAct; P36649; 5.
DR STRING; 511145.b0123; -.
DR TCDB; 1.B.76.1.8; the copper resistance putative porin (copb) family.
DR jPOST; P36649; -.
DR PaxDb; P36649; -.
DR PRIDE; P36649; -.
DR EnsemblBacteria; AAC73234; AAC73234; b0123.
DR EnsemblBacteria; BAB96698; BAB96698; BAB96698.
DR GeneID; 947736; -.
DR KEGG; ecj:JW0119; -.
DR KEGG; eco:b0123; -.
DR PATRIC; fig|1411691.4.peg.2159; -.
DR EchoBASE; EB2223; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_2_4_6; -.
DR InParanoid; P36649; -.
DR OMA; LLPKQWG; -.
DR PhylomeDB; P36649; -.
DR BioCyc; EcoCyc:EG12318-MON; -.
DR BioCyc; MetaCyc:EG12318-MON; -.
DR SABIO-RK; P36649; -.
DR EvolutionaryTrace; P36649; -.
DR PRO; PR:P36649; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:EcoCyc.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IDA:EcoliWiki.
DR GO; GO:0016724; F:oxidoreductase activity, acting on metal ions, oxygen as acceptor; IDA:EcoCyc.
DR GO; GO:0010273; P:detoxification of copper ion; IDA:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IMP:EcoCyc.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 29..516
FT /note="Multicopper oxidase CueO"
FT /id="PRO_0000002951"
FT DOMAIN 55..165
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 227..292
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 402..516
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 355..400
FT /note="Methionine-rich region"
FT /evidence="ECO:0000305|PubMed:11867755"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF,
FT ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV,
FT ECO:0007744|PDB:2YXW"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 141
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 143
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 443
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 446
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF,
FT ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV,
FT ECO:0007744|PDB:2YXW"
FT BINDING 448
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 499
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 500
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 501
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT BINDING 505
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:11867755,
FT ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912,
FT ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583,
FT ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7,
FT ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3,
FT ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE,
FT ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG,
FT ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW"
FT MUTAGEN 3
FT /note="R->K: Abolishes transport to periplasm."
FT /evidence="ECO:0000269|PubMed:10766774"
FT MUTAGEN 8
FT /note="K->A: Does not slow export to the periplasm."
FT /evidence="ECO:0000269|PubMed:10766774"
FT MUTAGEN 8
FT /note="K->R: Small increase in export rate."
FT /evidence="ECO:0000269|PubMed:10766774"
FT MUTAGEN 106
FT /note="E->F: Increases oxidase activity with ABTS as
FT substrate."
FT /evidence="ECO:0000269|PubMed:17217912"
FT MUTAGEN 304
FT /note="G->K: Retains 20% of cuprous oxidase activity.
FT Increases oxidase activity with ABTS as substrate. Shows
FT dramatic conformational changes in methionine-rich helix
FT and the relative regulatory loop."
FT /evidence="ECO:0000269|PubMed:30250139"
FT MUTAGEN 355
FT /note="M->L: Almost loss of oxidase activity with 2,6-DMP
FT as substrate. Loss of the copper tolerance phenotype."
FT /evidence="ECO:0000269|PubMed:12794077"
FT MUTAGEN 357..406
FT /note="Missing: Retains only 10% of cuprous oxidase
FT activity. 30-fold and 10-fold increase in activities with
FT ABTS and pPD, respectively, in the absence of exogenous
FT Cu(2+), but does not change these activities in the
FT presence of excess Cu(2+)."
FT /evidence="ECO:0000269|PubMed:17804014"
FT MUTAGEN 360
FT /note="D->A: Strong decrease in oxidase activity with 2,6-
FT DMP as substrate. Loss of the copper tolerance phenotype."
FT /evidence="ECO:0000269|PubMed:12794077"
FT MUTAGEN 439
FT /note="D->A: Decrease in oxidase activity with 2,6-DMP as
FT substrate."
FT /evidence="ECO:0000269|PubMed:12794077"
FT MUTAGEN 441
FT /note="M->L: Strong decrease in oxidase activity with 2,6-
FT DMP as substrate. Affects copper incorporation into the T1
FT copper site."
FT /evidence="ECO:0000269|PubMed:12794077"
FT MUTAGEN 500..501
FT /note="CH->SR: Residual DMP oxidase activity and loss of
FT resistance to copper. Decreases copper content."
FT /evidence="ECO:0000269|PubMed:11527384"
FT MUTAGEN 500
FT /note="C->S: Loss of cuprous oxidase activity."
FT /evidence="ECO:0000269|PubMed:15516598"
FT STRAND 47..59
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5YS1"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4E9S"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:4E9S"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:4E9S"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4E9S"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 314..325
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:3OD3"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:6IM9"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:6IM9"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 470..484
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:4E9S"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:4E9S"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:4E9S"
SQ SEQUENCE 516 AA; 56556 MW; 37D96B1C331CF30B CRC64;
MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG
GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP
PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD
VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN
ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV
SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD
MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP
MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS
EVLVKFNHDA PKEHAYMAHC HLLEHEDTGM MLGFTV
