ID A0A1X7AR11_9GAMM Unreviewed; 776 AA.
AC A0A1X7AR11;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Lead, cadmium, zinc and mercury-transporting ATPase {ECO:0000313|EMBL:SMA50583.1};
DE EC=3.6.3.3 {ECO:0000313|EMBL:SMA50583.1};
GN Name=zntA {ECO:0000313|EMBL:SMA50583.1};
GN ORFNames=EHSB41UT_04400 {ECO:0000313|EMBL:SMA50583.1};
OS Parendozoicomonas haliclonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Parendozoicomonas.
OX NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA50583.1, ECO:0000313|Proteomes:UP000196573};
RN [1] {ECO:0000313|EMBL:SMA50583.1, ECO:0000313|Proteomes:UP000196573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA50583.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWPT01000013; SMA50583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7AR11; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000196573; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd07546; P-type_ATPase_Pb_Zn_Cd2-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Hydrolase {ECO:0000313|EMBL:SMA50583.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000196573};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 386..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 413..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 742..764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 72..138
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 30..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 81793 MW; E170B2F7B98E6A87 CRC64;
MSSSCQSKGC HSSHCHAPAR AHVSHGAMSS IENSCDSAPT SSEHSSDGGG CCSVSDDGDP
ESEVSTLSTS KASHSWHIAG IDCPSCIKKV ETALARVHGV KTARVSFATM RLQVAFHSDQ
DNIPGVFACV EELGYQLSEL EAGPVKVEEP HFLKKYSSIL ILGALLGGGA MLSSVMPDIG
RLTLVLATLW GVYPIGRKAW SQARSGTPFG IETLMTVAAL GALFLGETLE AAMVLLLFMI
GEQLEGLAAS RARKGVESLM ALTPDKALRI HINDDGQEHR ESVLAERLTP GDIIEVMPGD
RLAADGQLVS PQASFDESAL TGESVPVDRQ AGETVMAGSL CVDRVVRLQV VSEPGQNAID
RIVKLIEDAD ESKAPIERFI DRFSRWYTPL IMSLSVLVIV VPPLLLGMDW ETWIYRGLTL
LLVGCPCALV ISTPAAVTSG LARAARQGIL IKGGAVLEQL GAVRQVAFDK TGTLTEGRPE
VVDLVALNGS SENLLAMAAA VEQGSRHPLA QAVVRYAGQQ AITIPVADDL EANVGRGVSG
RVNGNEVSVG SPAHLAELID ANANTHIARL EEQGCTVVGV ACDGQLLGVL AIRDTLRSDA
GDAVRALEQL GVQAIMLTGD NKRAAAAIAG ELGIAYRAGL LPEGKVTEVQ ALQRQSPVAM
VGDGINDAPA LKMADVGIAM GKGTDVALET ADAALTHERV QDLASMIDLS RATLNIVRQN
VFFAIGLKAV FLVTSLTGVT GLMLAVMADT GATALVTLNS LRLLRRRKLQ LRRRKL
//