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Zinc/cadmium/lead-transporting P-type ATPase (EC 3.6.3.-) (EC 3.6.3.3) (EC 3.6.3.5) (Zn(2 )/Cd(2 )/Pb(2 ) export ATPase)

 ZNTA_SHISS              Reviewed;         732 AA.
Q3YW59;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
28-MAR-2018, entry version 108.
RecName: Full=Zinc/cadmium/lead-transporting P-type ATPase {ECO:0000305};
EC=3.6.3.- {ECO:0000250|UniProtKB:P37617};
EC=3.6.3.3 {ECO:0000250|UniProtKB:P37617};
EC=3.6.3.5 {ECO:0000269|PubMed:25132545};
AltName: Full=Zn(2+)/Cd(2+)/Pb(2+) export ATPase {ECO:0000305};
Name=zntA {ECO:0000303|PubMed:25132545};
OrderedLocusNames=SSON_3707 {ECO:0000312|EMBL:AAZ90253.1};
Shigella sonnei (strain Ss046).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Shigella.
NCBI_TaxID=300269;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ss046;
PubMed=16275786; DOI=10.1093/nar/gki954;
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic
agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(2005).
[2] {ECO:0000244|PDB:4UMV, ECO:0000244|PDB:4UMW}
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
PHOSPHATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
METAL-BINDING SITES, AND MUTAGENESIS OF MET-187; GLU-202; PHE-210;
GLU-214; TYR-354; ASP-436; LYS-693 AND ASP-714.
PubMed=25132545; DOI=10.1038/nature13618;
Wang K., Sitsel O., Meloni G., Autzen H.E., Andersson M., Klymchuk T.,
Nielsen A.M., Rees D.C., Nissen P., Gourdon P.;
"Structure and mechanism of Zn2+-transporting P-type ATPases.";
Nature 514:518-522(2014).
-!- FUNCTION: Confers resistance to zinc, cadmium and lead. Couples
the hydrolysis of ATP with the export of zinc, cadmium or lead.
{ECO:0000305|PubMed:25132545}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Zn(2+)(In) = ADP + phosphate +
Zn(2+)(Out). {ECO:0000269|PubMed:25132545}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cd(2+)(In) = ADP + phosphate +
Cd(2+)(Out). {ECO:0000250|UniProtKB:P37617}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Pb(2+)(In) = ADP + phosphate +
Pb(2+)(Out). {ECO:0000250|UniProtKB:P37617}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000250|UniProtKB:P37617}; Multi-pass membrane protein
{ECO:0000255}.
-!- DOMAIN: Has two high-affinity metal-binding sites, one in the N-
terminal region and another in the transmembrane region. Both
sites are able to access and bind metal ion independently of each
other. The N-terminal metal-binding site is not strictly necessary
for activity and metal selectivity, but is needed for maximal
activity and may be involved in regulation. The metal-binding site
in the transmembrane region is essential for activity of the pump.
{ECO:0000250|UniProtKB:P37617}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000038; AAZ90253.1; -; Genomic_DNA.
PDB; 4UMV; X-ray; 3.20 A; A=1-732.
PDB; 4UMW; X-ray; 2.71 A; A=1-732.
PDBsum; 4UMV; -.
PDBsum; 4UMW; -.
ProteinModelPortal; Q3YW59; -.
SMR; Q3YW59; -.
EnsemblBacteria; AAZ90253; AAZ90253; SSON_3707.
KEGG; ssn:SSON_3707; -.
HOGENOM; HOG000250399; -.
KO; K01534; -.
OMA; AVVAKCC; -.
Proteomes; UP000002529; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008551; F:cadmium-exporting ATPase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016463; F:zinc-exporting ATPase activity; IEA:UniProtKB-EC.
CDD; cd00371; HMA; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 1.
PRINTS; PR00120; HATPASE.
SUPFAM; SSF55008; SSF55008; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 1.
PROSITE; PS50846; HMA_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cadmium; Cell inner membrane;
Cell membrane; Complete proteome; Hydrolase; Ion transport; Lead;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Transmembrane; Transmembrane helix; Transport; Zinc;
Zinc transport.
CHAIN 1 732 Zinc/cadmium/lead-transporting P-type
ATPase.
/FTId=PRO_0000439356.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000305}.
TRANSMEM 125 145 Helical. {ECO:0000255}.
TOPO_DOM 146 146 Periplasmic. {ECO:0000305}.
TRANSMEM 147 167 Helical. {ECO:0000255}.
TOPO_DOM 168 179 Cytoplasmic. {ECO:0000305}.
TRANSMEM 180 197 Helical. {ECO:0000255}.
TOPO_DOM 198 202 Periplasmic. {ECO:0000305}.
TRANSMEM 203 222 Helical. {ECO:0000255}.
TOPO_DOM 223 356 Cytoplasmic. {ECO:0000305}.
TRANSMEM 357 377 Helical. {ECO:0000255}.
TOPO_DOM 378 383 Periplasmic. {ECO:0000305}.
TRANSMEM 384 404 Helical. {ECO:0000255}.
TOPO_DOM 405 685 Cytoplasmic. {ECO:0000305}.
TRANSMEM 686 702 Helical. {ECO:0000255}.
TOPO_DOM 703 707 Periplasmic. {ECO:0000305}.
TRANSMEM 708 729 Helical. {ECO:0000255}.
TOPO_DOM 730 732 Cytoplasmic.
{ECO:0000250|UniProtKB:P37617}.
DOMAIN 49 113 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
ACT_SITE 436 436 4-aspartylphosphate intermediate.
{ECO:0000305|PubMed:25132545}.
METAL 58 58 Zinc 1. {ECO:0000250|UniProtKB:P37617}.
METAL 59 59 Zinc 1. {ECO:0000250|UniProtKB:P37617}.
METAL 62 62 Zinc 1. {ECO:0000250|UniProtKB:P37617}.
METAL 392 392 Zinc 2. {ECO:0000250|UniProtKB:P37617}.
METAL 394 394 Zinc 2. {ECO:0000250|UniProtKB:P37617}.
METAL 436 436 Magnesium. {ECO:0000269|PubMed:25132545}.
METAL 438 438 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:25132545}.
METAL 628 628 Magnesium. {ECO:0000269|PubMed:25132545}.
METAL 714 714 Zinc 2. {ECO:0000250|UniProtKB:P37617,
ECO:0000305|PubMed:25132545}.
SITE 693 693 Important for metal transport.
{ECO:0000305|PubMed:25132545}.
MUTAGEN 187 187 M->A: No change in ATPase activity and in
zinc binding.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 202 202 E->A: Lack of ATPase activity and
decrease in zinc binding.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 202 202 E->D: Lack of ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 202 202 E->Q: Strong decrease in ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 210 210 F->A: Decrease in ATPase activity and
slight decrease in zinc binding.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 214 214 E->A,Q: Decrease in ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 354 354 Y->A,F: Decrease in ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 436 436 D->N: Lack of ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 693 693 K->A: Lack of ATPase activity but does
not affect zinc binding.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 693 693 K->R: Lack of ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 714 714 D->E: Strong decrease in ATPase activity.
{ECO:0000269|PubMed:25132545}.
MUTAGEN 714 714 D->N: Lack of ATPase activity and strong
decrease in zinc binding.
{ECO:0000269|PubMed:25132545}.
HELIX 129 144 {ECO:0000244|PDB:4UMW}.
STRAND 146 148 {ECO:0000244|PDB:4UMV}.
HELIX 149 176 {ECO:0000244|PDB:4UMW}.
HELIX 183 196 {ECO:0000244|PDB:4UMW}.
HELIX 200 219 {ECO:0000244|PDB:4UMW}.
HELIX 229 232 {ECO:0000244|PDB:4UMW}.
STRAND 237 243 {ECO:0000244|PDB:4UMW}.
STRAND 246 251 {ECO:0000244|PDB:4UMW}.
TURN 252 254 {ECO:0000244|PDB:4UMW}.
STRAND 260 263 {ECO:0000244|PDB:4UMW}.
STRAND 273 275 {ECO:0000244|PDB:4UMW}.
STRAND 277 283 {ECO:0000244|PDB:4UMW}.
HELIX 285 288 {ECO:0000244|PDB:4UMW}.
STRAND 294 297 {ECO:0000244|PDB:4UMW}.
STRAND 313 317 {ECO:0000244|PDB:4UMW}.
HELIX 321 323 {ECO:0000244|PDB:4UMV}.
HELIX 325 338 {ECO:0000244|PDB:4UMW}.
HELIX 346 372 {ECO:0000244|PDB:4UMW}.
HELIX 377 391 {ECO:0000244|PDB:4UMW}.
HELIX 396 413 {ECO:0000244|PDB:4UMW}.
STRAND 416 418 {ECO:0000244|PDB:4UMV}.
HELIX 421 428 {ECO:0000244|PDB:4UMW}.
STRAND 432 435 {ECO:0000244|PDB:4UMW}.
TURN 439 441 {ECO:0000244|PDB:4UMW}.
STRAND 442 453 {ECO:0000244|PDB:4UMW}.
HELIX 459 470 {ECO:0000244|PDB:4UMW}.
HELIX 476 487 {ECO:0000244|PDB:4UMW}.
STRAND 496 501 {ECO:0000244|PDB:4UMW}.
TURN 502 504 {ECO:0000244|PDB:4UMW}.
STRAND 505 510 {ECO:0000244|PDB:4UMW}.
STRAND 513 519 {ECO:0000244|PDB:4UMW}.
STRAND 520 523 {ECO:0000244|PDB:4UMV}.
HELIX 526 528 {ECO:0000244|PDB:4UMV}.
HELIX 529 537 {ECO:0000244|PDB:4UMW}.
STRAND 541 547 {ECO:0000244|PDB:4UMW}.
STRAND 550 561 {ECO:0000244|PDB:4UMW}.
HELIX 565 574 {ECO:0000244|PDB:4UMW}.
STRAND 578 582 {ECO:0000244|PDB:4UMW}.
HELIX 587 597 {ECO:0000244|PDB:4UMW}.
STRAND 600 602 {ECO:0000244|PDB:4UMW}.
HELIX 607 620 {ECO:0000244|PDB:4UMW}.
STRAND 623 627 {ECO:0000244|PDB:4UMW}.
HELIX 630 632 {ECO:0000244|PDB:4UMW}.
HELIX 633 638 {ECO:0000244|PDB:4UMW}.
STRAND 639 645 {ECO:0000244|PDB:4UMW}.
HELIX 650 655 {ECO:0000244|PDB:4UMW}.
STRAND 657 660 {ECO:0000244|PDB:4UMW}.
HELIX 666 701 {ECO:0000244|PDB:4UMW}.
HELIX 707 725 {ECO:0000244|PDB:4UMW}.
HELIX 726 729 {ECO:0000244|PDB:4UMW}.
SEQUENCE 732 AA; 76767 MW; 115E513DD79413EA CRC64;
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSSPT LSENVSGTRY SWKVSGMDCA
ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV ESAVQKAGYS LRDEQAADEP
QASRLKENLP LITLIVMMAI SWGLEQFNHP FGQLAFIATT LVGLYPIARQ ALRLIKSGSY
FAIETLMSVA AIGALFIGAT AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT
RLRNGEREEV 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 GKHPADAFAG LINELESAGQ
TVVLVVRNDD VLGIIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
FKAGLLPEDK VKAVTKLNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD VALETADAAL
THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT LLGMTGLWLA VLADTGATVL
VTANALRLLR RR


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