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Database: UniProt
Entry: A0A166RWE2_9EURY
LinkDB: A0A166RWE2_9EURY
Original site: A0A166RWE2_9EURY 
ID   A0A166RWE2_9EURY        Unreviewed;       840 AA.
AC   A0A166RWE2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE            EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE   AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN   ORFNames=A4G99_15145 {ECO:0000313|EMBL:KZN23457.1};
OS   Haladaptatus sp. R4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haladaptataceae; Haladaptatus.
OX   NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN23457.1, ECO:0000313|Proteomes:UP000076599};
RN   [1] {ECO:0000313|EMBL:KZN23457.1, ECO:0000313|Proteomes:UP000076599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4 {ECO:0000313|EMBL:KZN23457.1,
RC   ECO:0000313|Proteomes:UP000076599};
RA   Mukhopadhyay S.K.;
RT   "Genome sequence of halophilic archaea.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC       {ECO:0000256|ARBA:ARBA00003954}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC         Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00001857};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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:KZN23457.1}.
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DR   EMBL; LWHG01000029; KZN23457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166RWE2; -.
DR   STRING; 1679489.A4G99_15145; -.
DR   OrthoDB; 8588at2157; -.
DR   Proteomes; UP000076599; Unassembled WGS sequence.
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:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006415; P-type_ATPase_IIIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01524; ATPase-IIIB_Mg; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR01836; MGATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        666..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        716..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        749..766
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        778..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        810..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..79
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   840 AA;  92614 MW;  E1E0E107F6F06FDD CRC64;
     MQRELSFWSE SVDDLFAELD TTRAGLSTET ARQRLEAYGY NRFQRKERLS VVRLFARQFK
     SAIVLLLLFA AVLSFLLGER TETWIIFAIV LLSGLLGFWQ EYNATNAVEE LLSLVEVEAE
     VVRDGEPSAV KIDDVVPGDI TRLNAGDTIP GDCRLLEAES LHVNEAVLTG ETFPVEKTPG
     TVSPTAPIAD RTNSLFMGTH VVSGEATAVV VRTGERTELG QISERLQYRP PETDFERGIR
     HFGHLLLEVT LLLVLAIFAI NVYFQRPIFD SFLFALALAV GLTPQLLPAI ITINLASGAR
     DMATENVIVK QPSAIENFGS MDVFCADKTG TLTEGTIRVH SAIDIDGNES ERTFLHAYLN
     SSYESGFENP IDEAVREADD IDTTPYRKLG EVPYDFTRKR LSVLLADRDE SRLITKGAVE
     NVLDVCTTAE TASGDAVPIS EAEPSIRDEF EAASEDGFRV LGVATRTWEE KRQVTRADEA
     GVTFLGLLLL EDPPKDGIAE TVRDLESLGV GLKIISGDNR YVVHHVGELV GLADERQVLT
     GTDIAGMSDD ALRARIDRVN LFAEVEPSQK ERIIVALQDQ GHVVGYLGDG INDAPSLRAA
     DAGISVDSAV DVAKEAANIV LLERNLSVLV DGIRSGRRTF MNTLKYIFLT TSANFGNMFS
     MAGASLFLPF LPLLPVQILL INLLSDLPAI TISTDTVDSE WVDTPRRWNI SFIRDFMVTF
     GTVSSVFDFF TFGVLLIGLR ATVTEFRTGW FVFSVLTEVL MVLLIRTRKP IFESRPSGPL
     VVASLAIALL TPLFPMLFIG RVFDFTPLTI PLFVALLGLL VGYLLTIEVV KRVFYRHISL
//
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