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Database: UniProt
Entry: A0A1I5H7I4_PARPN
LinkDB: A0A1I5H7I4_PARPN
Original site: A0A1I5H7I4_PARPN 
ID   A0A1I5H7I4_PARPN        Unreviewed;       724 AA.
AC   A0A1I5H7I4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cd2+/Zn2+-exporting ATPase {ECO:0000313|EMBL:RKS51363.1};
GN   ORFNames=BDE18_0609 {ECO:0000313|EMBL:RKS51363.1};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=82367 {ECO:0000313|EMBL:RKS51363.1, ECO:0000313|Proteomes:UP000273626};
RN   [1] {ECO:0000313|EMBL:RKS51363.1, ECO:0000313|Proteomes:UP000273626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC   NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKS51363.1}.
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DR   EMBL; RBLI01000001; RKS51363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5H7I4; -.
DR   Proteomes; UP000273626; 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; 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   PRINTS; PR00941; CDATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; PS01229; COF_2; 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   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   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        110..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        369..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        673..698
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          5..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          77..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  74513 MW;  E4E919FD336779CF CRC64;
     MEQAQRREWT VTGMDCASCS AKVMRAVERL PGVSEVSVAL MAERLALTLT PGTTAEAEIE
     GVVRKLGYNI APKGPGAPGP ALPDAPAAAS HPGVPVRPDR GESWHRTGKG RLVILTGLLL
     AVAWGLELLA PAAAGQWAFL AACLIGVAPV TRRALAALRM GQPFTIEALM TIAALGALVI
     GAAQEAALVV FLFALGELLE GVAAGKARDG IRALADLVPR TALLEIDGGG TREIPADRLA
     IGQVVLVRPG DRIPADGEIV AGISGLDESP VTGESLPRSR GPGEPVLAGS INTEAALRIR
     VTRAPSDNTI ARIIRLVEQA EESRAPTERF IDRFSRWYMP AVVAAAALAM LVPPLGFGAD
     WDTWIYRGLA LLLIGCPCAL VISVPASIAS ALSSGARRGL LMKGGAVIEA AAHVRHLAFD
     KTGTLTLGRP AVVRILPAPG VTEAALLAAA AGVEAGSSHP LAQAILRRAA EAGIAPLPAH
     AARALPGQGV EAMLGQTRAW VAAPRHAAAM GGLRDASEAE GMEAQGMTVV AVFDQHRPLG
     LIALRDEPRP DAAEALRQLK AMGIEATMLT GDNPRTAQAI AGALGLGFRA GMLPADKLEA
     IRDMAAQGGV MMIGDGINDA PALKQASVGV AMGSGTDVAL ETADAAILRD RVTDVPALIR
     LARTTMANIR QNIAIALGLK AVFLVTSVLG ITGLWIAILA DTGATVLVTL NALRLLGHDP
     GKAG
//
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