ZNTA_SHISS
ID ZNTA_SHISS Reviewed; 732 AA.
AC Q3YW59;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zinc/cadmium/lead-transporting P-type ATPase {ECO:0000305};
DE EC=7.2.2.- {ECO:0000250|UniProtKB:P37617};
DE EC=7.2.2.12 {ECO:0000269|PubMed:25132545};
DE EC=7.2.2.21 {ECO:0000250|UniProtKB:P37617};
DE AltName: Full=Zn(2+)/Cd(2+)/Pb(2+) export ATPase {ECO:0000305};
GN Name=zntA {ECO:0000303|PubMed:25132545};
GN OrderedLocusNames=SSON_3707 {ECO:0000312|EMBL:AAZ90253.1};
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
RN [2] {ECO:0007744|PDB:4UMV, ECO:0007744|PDB:4UMW}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP PHOSPHATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, METAL-BINDING
RP SITES, AND MUTAGENESIS OF MET-187; GLU-202; PHE-210; GLU-214; TYR-354;
RP ASP-436; LYS-693 AND ASP-714.
RX PubMed=25132545; DOI=10.1038/nature13618;
RA Wang K., Sitsel O., Meloni G., Autzen H.E., Andersson M., Klymchuk T.,
RA Nielsen A.M., Rees D.C., Nissen P., Gourdon P.;
RT "Structure and mechanism of Zn2+-transporting P-type ATPases.";
RL Nature 514:518-522(2014).
CC -!- FUNCTION: Confers resistance to zinc, cadmium and lead. Couples the
CC hydrolysis of ATP with the export of zinc, cadmium or lead.
CC {ECO:0000305|PubMed:25132545}.
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:0000250|UniProtKB:P37617};
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:25132545};
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:0000250|UniProtKB:P37617};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P37617}; Multi-pass membrane protein
CC {ECO:0000255}.
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:0000250|UniProtKB:P37617}.
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; CP000038; AAZ90253.1; -; Genomic_DNA.
DR PDB; 4UMV; X-ray; 3.20 A; A=1-732.
DR PDB; 4UMW; X-ray; 2.71 A; A=1-732.
DR PDBsum; 4UMV; -.
DR PDBsum; 4UMW; -.
DR AlphaFoldDB; Q3YW59; -.
DR SMR; Q3YW59; -.
DR EnsemblBacteria; AAZ90253; AAZ90253; SSON_3707.
DR KEGG; ssn:SSON_3707; -.
DR HOGENOM; CLU_001771_6_4_6; -.
DR OMA; FAQPWET; -.
DR BRENDA; 7.2.2.12; 5713.
DR Proteomes; UP000002529; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
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; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..732
FT /note="Zinc/cadmium/lead-transporting P-type ATPase"
FT /id="PRO_0000439356"
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:0000250|UniProtKB:P37617"
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:0000305|PubMed:25132545"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P37617"
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 BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P37617"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P37617"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25132545"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25132545"
FT BINDING 628
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25132545"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P37617,
FT ECO:0000305|PubMed:25132545"
FT SITE 693
FT /note="Important for metal transport"
FT /evidence="ECO:0000305|PubMed:25132545"
FT MUTAGEN 187
FT /note="M->A: No change in ATPase activity and in zinc
FT binding."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 202
FT /note="E->A: Lack of ATPase activity and decrease in zinc
FT binding."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 202
FT /note="E->D: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 202
FT /note="E->Q: Strong decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 210
FT /note="F->A: Decrease in ATPase activity and slight
FT decrease in zinc binding."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 214
FT /note="E->A,Q: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 354
FT /note="Y->A,F: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 436
FT /note="D->N: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 693
FT /note="K->A: Lack of ATPase activity but does not affect
FT zinc binding."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 693
FT /note="K->R: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 714
FT /note="D->E: Strong decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:25132545"
FT MUTAGEN 714
FT /note="D->N: Lack of ATPase activity and strong decrease in
FT zinc binding."
FT /evidence="ECO:0000269|PubMed:25132545"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4UMV"
FT HELIX 149..176
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4UMW"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:4UMV"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 346..372
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 396..413
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:4UMV"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:4UMW"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 442..453
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:4UMW"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:4UMV"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:4UMV"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 550..561
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 565..574
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 587..597
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 607..620
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 633..638
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 650..655
FT /evidence="ECO:0007829|PDB:4UMW"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 666..701
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 707..725
FT /evidence="ECO:0007829|PDB:4UMW"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:4UMW"
SQ 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
