ZNTA_ECOLI
ID ZNTA_ECOLI Reviewed; 732 AA.
AC P37617; Q2M7D2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc/cadmium/lead-transporting P-type ATPase {ECO:0000305};
DE EC=7.2.2.- {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661};
DE EC=7.2.2.12 {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661, ECO:0000269|PubMed:9405611};
DE EC=7.2.2.21 {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661, ECO:0000269|PubMed:9405611};
DE AltName: Full=Pb(II)/Cd(II)/Zn(II)-translocating ATPase {ECO:0000303|PubMed:10660539};
DE AltName: Full=Zn(2+)/Cd(2+)/Pb(2+) export ATPase {ECO:0000305};
GN Name=zntA {ECO:0000303|PubMed:9364914, ECO:0000303|PubMed:9405611};
GN Synonyms=yhhO; OrderedLocusNames=b3469, JW3434;
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 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(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].
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9405611; DOI=10.1073/pnas.94.26.14326;
RA Rensing C., Mitra B., Rosen B.P.;
RT "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type
RT ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9364914; DOI=10.1111/j.1365-2958.1997.mmi518.x;
RA Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K.;
RT "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene
RT (o732) encodes a cation transport ATPase.";
RL Mol. Microbiol. 25:883-891(1997).
RN [6]
RP FUNCTION IN PB(2+) RESISTANCE, AND DISRUPTION PHENOTYPE.
RX PubMed=9830000; DOI=10.1074/jbc.273.49.32614;
RA Rensing C., Sun Y., Mitra B., Rosen B.P.;
RT "Pb(II)-translocating P-type ATPases.";
RL J. Biol. Chem. 273:32614-32617(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10660539; DOI=10.1074/jbc.275.6.3873;
RA Sharma R., Rensing C., Rosen B.P., Mitra B.;
RT "The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-
RT translocating ATPase from Escherichia coli.";
RL J. Biol. Chem. 275:3873-3878(2000).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 SUBCELLULAR LOCATION, DOMAIN, METAL-BINDING SITES, AND MUTAGENESIS OF
RP 59-CYS--CYS-62 AND 392-CYS--CYS-394.
RX PubMed=16411752; DOI=10.1021/bi051836n;
RA Liu J., Dutta S.J., Stemmler A.J., Mitra B.;
RT "Metal-binding affinity of the transmembrane site in ZntA: implications for
RT metal selectivity.";
RL Biochemistry 45:763-772(2006).
RN [10]
RP SUBCELLULAR LOCATION, DOMAIN, METAL-BINDING SITES, AND MUTAGENESIS OF
RP 59-CYS--CYS-62; 392-CYS--CYS-394; LYS-693 AND ASP-714.
RX PubMed=16890908; DOI=10.1016/j.bbabio.2006.06.008;
RA Okkeri J., Haltia T.;
RT "The metal-binding sites of the zinc-transporting P-type ATPase of
RT Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane
RT segments of ZntA contribute to the coupling of metal binding and ATPase
RT activity.";
RL Biochim. Biophys. Acta 1757:1485-1495(2006).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN,
RP METAL-BINDING SITES, AND MUTAGENESIS OF CYS-392; PRO-393 AND CYS-394.
RX PubMed=17326661; DOI=10.1021/bi0616394;
RA Dutta S.J., Liu J., Stemmler A.J., Mitra B.;
RT "Conservative and nonconservative mutations of the transmembrane CPC motif
RT in ZntA: effect on metal selectivity and activity.";
RL Biochemistry 46:3692-3703(2007).
RN [12]
RP METAL-BINDING SITES.
RX PubMed=22387457; DOI=10.1016/j.bbamem.2012.02.020;
RA Raimunda D., Subramanian P., Stemmler T., Argueello J.M.;
RT "A tetrahedral coordination of zinc during transmembrane transport by P-
RT type Zn(2+)-ATPases.";
RL Biochim. Biophys. Acta 1818:1374-1377(2012).
RN [13] {ECO:0007744|PDB:1MWY, ECO:0007744|PDB:1MWZ}
RP STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.
RX PubMed=12417201; DOI=10.1016/s0022-2836(02)01007-0;
RA Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E.,
RA O'Halloran T.V.;
RT "A new zinc-protein coordination site in intracellular metal trafficking:
RT solution structure of the Apo and Zn(II) forms of ZntA(46-118).";
RL J. Mol. Biol. 323:883-897(2002).
CC -!- FUNCTION: Confers resistance to zinc, cadmium and lead (PubMed:9405611,
CC PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661).
CC Couples the hydrolysis of ATP with the export of zinc, cadmium or lead,
CC with highest activity when the metals are present as metal-thiolate
CC complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also
CC bind nickel, copper, cobalt and mercury (PubMed:10660539,
CC PubMed:17326661). {ECO:0000269|PubMed:10660539,
CC ECO:0000269|PubMed:17326661, ECO:0000269|PubMed:9364914,
CC ECO:0000269|PubMed:9405611, ECO:0000269|PubMed:9830000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Pb(2+)(in) = ADP + H(+) + Pb(2+)(out) + phosphate;
CC Xref=Rhea:RHEA:52580, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49807,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10660539,
CC ECO:0000269|PubMed:17326661};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC Evidence={ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661,
CC ECO:0000269|PubMed:9405611};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC Evidence={ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661,
CC ECO:0000269|PubMed:9405611};
CC -!- ACTIVITY REGULATION: Inhibited by orthovanadate.
CC {ECO:0000269|PubMed:9405611}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for Pb(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10660539};
CC KM=6.1 uM for Pb(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=118 uM for Pb(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10660539};
CC KM=150 uM for Pb(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=5.1 uM for Zn(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661};
CC KM=109 uM for Zn(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10660539};
CC KM=105 uM for Zn(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=3.1 uM for Cd(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=115 uM for Cd(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:10660539};
CC KM=123 uM for Cd(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=3.4 uM for Cu(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=85 uM for Cu(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=2.1 uM for Ni(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=169 uM for Ni(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=4.0 uM for Co(2+) (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC KM=75 uM for Co(2+)-thiolate (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17326661};
CC Vmax=0.88 umol/min/mg enzyme with Pb(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:10660539};
CC Vmax=0.638 umol/min/mg enzyme with Pb(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=3.02 umol/min/mg enzyme with Pb(2+)-thiolate as substrate (at 37
CC degrees Celsius and pH 7.0) {ECO:0000269|PubMed:10660539};
CC Vmax=2.497 umol/min/mg enzyme with Pb(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.19 umol/min/mg enzyme with Zn(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:10660539};
CC Vmax=0.21 umol/min/mg enzyme with Zn(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.96 umol/min/mg enzyme with Zn(2+)-thiolate as substrate (at 37
CC degrees Celsius and pH 7.0) {ECO:0000269|PubMed:10660539};
CC Vmax=0.932 umol/min/mg enzyme with Zn(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.102 umol/min/mg enzyme with Cd(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=1.16 umol/min/mg enzyme with Cd(2+)-thiolate as substrate (at 37
CC degrees Celsius and pH 7.0) {ECO:0000269|PubMed:10660539};
CC Vmax=0.862 umol/min/mg enzyme with Cd(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.085 umol/min/mg enzyme with Cu(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.104 umol/min/mg enzyme with Cu(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.076 umol/min/mg enzyme with Ni(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.138 umol/min/mg enzyme with Ni(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.036 umol/min/mg enzyme with Co(2+) as substrate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC Vmax=0.103 umol/min/mg enzyme with Co(2+)-thiolate as substrate (at
CC 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:17326661};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10660539,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16411752,
CC ECO:0000269|PubMed:16890908}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by zinc. {ECO:0000269|PubMed:9405611}.
CC -!- DOMAIN: Has two high-affinity metal-binding sites, one in the N-
CC terminal region and another in the transmembrane region. Both sites are
CC able to access and bind metal ion independently of each other. The N-
CC terminal metal-binding site is not strictly necessary for activity and
CC metal selectivity, but is needed for maximal activity and may be
CC involved in regulation. The metal-binding site in the transmembrane
CC region is essential for activity of the pump.
CC {ECO:0000269|PubMed:16411752, ECO:0000269|PubMed:16890908,
CC ECO:0000269|PubMed:17326661}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits hypersensitivity to zinc,
CC cadmium, lead and, to a lesser extent, cobalt and nickel.
CC {ECO:0000269|PubMed:9364914, ECO:0000269|PubMed:9405611,
CC ECO:0000269|PubMed:9830000}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; U00039; AAB18444.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76494.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77824.1; -; Genomic_DNA.
DR PIR; S47688; S47688.
DR RefSeq; NP_417926.1; NC_000913.3.
DR RefSeq; WP_000106551.1; NZ_SSZK01000008.1.
DR PDB; 1MWY; NMR; -; A=46-118.
DR PDB; 1MWZ; NMR; -; A=46-118.
DR PDBsum; 1MWY; -.
DR PDBsum; 1MWZ; -.
DR AlphaFoldDB; P37617; -.
DR BMRB; P37617; -.
DR SMR; P37617; -.
DR BioGRID; 4262921; 26.
DR DIP; DIP-12947N; -.
DR IntAct; P37617; 8.
DR STRING; 511145.b3469; -.
DR TCDB; 3.A.3.6.2; the p-type atpase (p-atpase) superfamily.
DR jPOST; P37617; -.
DR PaxDb; P37617; -.
DR PRIDE; P37617; -.
DR EnsemblBacteria; AAC76494; AAC76494; b3469.
DR EnsemblBacteria; BAE77824; BAE77824; BAE77824.
DR GeneID; 947972; -.
DR KEGG; ecj:JW3434; -.
DR KEGG; eco:b3469; -.
DR PATRIC; fig|1411691.4.peg.3256; -.
DR EchoBASE; EB2129; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_4_6; -.
DR InParanoid; P37617; -.
DR OMA; FAQPWET; -.
DR PhylomeDB; P37617; -.
DR BioCyc; EcoCyc:YHHO-MON; -.
DR BioCyc; MetaCyc:YHHO-MON; -.
DR SABIO-RK; P37617; -.
DR EvolutionaryTrace; P37617; -.
DR PRO; PR:P37617; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISA:EcoliWiki.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015094; F:lead ion transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IDA:EcoCyc.
DR GO; GO:0016463; F:P-type zinc transporter activity; IDA:EcoCyc.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070574; P:cadmium ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0010312; P:detoxification of zinc ion; IMP:EcoliWiki.
DR GO; GO:0015692; P:lead ion transport; IMP:EcoCyc.
DR GO; GO:0046686; P:response to cadmium ion; IMP:EcoCyc.
DR GO; GO:0010288; P:response to lead ion; IEP:EcoCyc.
DR GO; GO:0010043; P:response to zinc ion; IMP:EcoCyc.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006829; P:zinc ion transport; IMP:EcoliWiki.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cadmium; Cell inner membrane; Cell membrane;
KW Ion transport; Lead; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..732
FT /note="Zinc/cadmium/lead-transporting P-type ATPase"
FT /id="PRO_0000046332"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..202
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..383
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 686..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..707
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 708..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 48..112
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 436
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q3YW59"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12417201"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12417201, ECO:0000305|PubMed:16411752,
FT ECO:0000305|PubMed:16890908"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12417201, ECO:0000305|PubMed:16411752,
FT ECO:0000305|PubMed:16890908"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16411752,
FT ECO:0000305|PubMed:16890908, ECO:0000305|PubMed:17326661,
FT ECO:0000305|PubMed:22387457"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16411752,
FT ECO:0000305|PubMed:16890908, ECO:0000305|PubMed:17326661,
FT ECO:0000305|PubMed:22387457"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q3YW59"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q3YW59"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q3YW59"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16890908,
FT ECO:0000305|PubMed:22387457"
FT SITE 693
FT /note="Important for metal transport"
FT /evidence="ECO:0000250|UniProtKB:Q3YW59,
FT ECO:0000305|PubMed:16890908, ECO:0000305|PubMed:22387457"
FT MUTAGEN 59..62
FT /note="CAAC->AAAA: 2-3-fold decrease in ATPase activity.
FT Binds metal ion only at the transmembrane site."
FT /evidence="ECO:0000269|PubMed:16411752"
FT MUTAGEN 59..62
FT /note="CAAC->SAAS: Reduces the ATPase activity by 50%.
FT Reduces level of phosphorylation."
FT /evidence="ECO:0000269|PubMed:16890908"
FT MUTAGEN 392..394
FT /note="CPC->APA: Lack of ATPase activity. Binds metal ion
FT only at the N-terminal site."
FT /evidence="ECO:0000269|PubMed:16411752"
FT MUTAGEN 392..394
FT /note="CPC->SPS: Lack of ATPase activity. Loss of zinc-
FT stimulated phosphorylation."
FT /evidence="ECO:0000269|PubMed:16890908"
FT MUTAGEN 392
FT /note="C->A: Lack of activity. Cannot bind metal at the
FT transmembrane site. Lack of phosphorylation with ATP."
FT /evidence="ECO:0000269|PubMed:17326661"
FT MUTAGEN 392
FT /note="C->H,S: Decrease in activity. Binds Zn(2+), Cd(2+),
FT Ni(2+), Co(2+) and Cu(2+), but not Pb(2+)."
FT /evidence="ECO:0000269|PubMed:17326661"
FT MUTAGEN 393
FT /note="P->A: Lack of activity with any metal. Cannot bind
FT metal at the transmembrane site. Lack of phosphorylation
FT with ATP."
FT /evidence="ECO:0000269|PubMed:17326661"
FT MUTAGEN 394
FT /note="C->A: Lack of activity. Cannot bind metal at the
FT transmembrane site. Lack of phosphorylation with ATP."
FT /evidence="ECO:0000269|PubMed:17326661"
FT MUTAGEN 394
FT /note="C->H,S: Decrease in activity. Binds Zn(2+), Cd(2+),
FT Ni(2+), Co(2+) and Cu(2+), but not Pb(2+)."
FT /evidence="ECO:0000269|PubMed:17326661"
FT MUTAGEN 693
FT /note="K->N: Loss of zinc-stimulated ATPase activity.
FT Poorly phosphorylated with ATP."
FT /evidence="ECO:0000269|PubMed:16890908"
FT MUTAGEN 714
FT /note="D->M: Shows high metal-independent ATPase activity.
FT Poorly phosphorylated with ATP."
FT /evidence="ECO:0000269|PubMed:16890908"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:1MWY"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1MWY"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1MWY"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1MWY"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1MWY"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1MWY"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1MWY"
SQ SEQUENCE 732 AA; 76840 MW; 25476EA830786465 CRC64;
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY SWKVSGMDCA
ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV ESALQKAGYS LRDEQAAEEP
QASRLKENLP LITLIVMMAI SWGLEQFNHP FGQLAFIATT LVGLYPIARQ ALRLIKSGSY
FAIETLMSVA AIGALFIGAT AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT
RLRKGEREEV AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF SRIYTPAIMA
VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST PAAITSGLAA AARRGALIKG
GAALEQLGRV TQVAFDKTGT LTVGKPRVTA IHPATGISES ELLTLAAAVE QGATHPLAQA
IVREAQVAEL AIPTAESQRA LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ
TVVLVVRNDD VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD VALETADAAL
THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT LLGMTGLWLA VLADTGATVL
VTANALRLLR RR
