ATZN_SYNY3
ID ATZN_SYNY3 Reviewed; 721 AA.
AC Q59998;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc-transporting ATPase;
DE EC=7.2.2.12;
DE AltName: Full=Zn(2+)-translocating P-type ATPase;
GN Name=ziaA; OrderedLocusNames=slr0798;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9724772; DOI=10.1073/pnas.95.18.10728;
RA Thelwell C., Robinson N.J., Turner-Cavet J.S.;
RT "An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc
RT exporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10728-10733(1998).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; BA000022; BAA10707.1; -; Genomic_DNA.
DR PIR; S77015; S77015.
DR PDB; 2LDI; NMR; -; A=6-111.
DR PDB; 2OFG; NMR; -; X=1-111.
DR PDB; 2OFH; NMR; -; X=1-111.
DR PDBsum; 2LDI; -.
DR PDBsum; 2OFG; -.
DR PDBsum; 2OFH; -.
DR AlphaFoldDB; Q59998; -.
DR SMR; Q59998; -.
DR IntAct; Q59998; 25.
DR STRING; 1148.1001826; -.
DR PaxDb; Q59998; -.
DR EnsemblBacteria; BAA10707; BAA10707; BAA10707.
DR KEGG; syn:slr0798; -.
DR eggNOG; COG2217; Bacteria.
DR InParanoid; Q59998; -.
DR OMA; AQVVIMN; -.
DR PhylomeDB; Q59998; -.
DR EvolutionaryTrace; Q59998; -.
DR Proteomes; UP000001425; 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:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
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; PR00941; CDATPASE.
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; Cell membrane; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc transport.
FT CHAIN 1..721
FT /note="Zinc-transporting ATPase"
FT /id="PRO_0000046333"
FT TOPO_DOM 1..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 129..140
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 161..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..190
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 364..369
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 370..387
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 388..671
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 672..693
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 694..701
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 702..717
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 718..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 8..74
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 618
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:2LDI"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2LDI"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2LDI"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2LDI"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2LDI"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2LDI"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2LDI"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2LDI"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2LDI"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2LDI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2LDI"
SQ SEQUENCE 721 AA; 76884 MW; BE187EB3900EC58B CRC64;
MTQSSPLKTQ QMQVGGMDCT SCKLKIEGSL ERLKGVAEAS VTVATGRLTV TYDPKQVSEI
TIQERIAALG YTLAEPKSSV TLNGHKHPHS HREEGHSHSH GAGEFNLKQE LLPVLTAIAL
FTIAILFEQP LHNTPGQIAE FAVIIPAYLL SGWTVLKTAG RNILRGQIFD ENFLMTIATL
GALAIHQLPE AVAVMLFFRV GELFQEYSVG RSRRSIKALL EARPDTANLK RNGTVQQVSP
ETVQVDDLIL VKPGEKVPLD GEILGGTSQV DTSALTGESV PGTVKPGDTI LAGMINQSGV
LTIRVTKLFS ESSIAKVLDL VENASSKKAS TEKFITQFAR YYTPVIVFLS LAVALLPPLF
IPGADRADWV YRALVLLVIS CPCGLVISIP LGYFGGIGGA AKHGILIKGS TFLDSLTAVK
TVVFDKTGTL TKGTFKVTQV VTKNGFSESE LLTLAAKAES HSTHPIALSI REAYAQSIAD
SEVADYEEIA GHGIRAVVQN QVVIAGNDRL LHREKIDHDT CDVAGTVVHL AVDGRYGGYI
LIADEIKEDA VQAIRDLKRM GVEKTVMLTG DSEIVAQSVA QQIGLDAFVA ELLPEEKVDE
IEQLLDPSGK AKLAFVGDGI NDAPVIARAD VGIAMGGLGS DAAIETADVV LMTDAPSKVA
EAIHVARKTR QIVVQNIVLA LGIKALFIAL GTIGLATLWE AVFADVGVAL LAILNATRIA
K
