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Database: UniProt
Entry: A0A1X7AR11_9GAMM
LinkDB: A0A1X7AR11_9GAMM
Original site: A0A1X7AR11_9GAMM 
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}.
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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
//
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