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Database: UniProt
Entry: A0A9W6GRP9_9HYPH
LinkDB: A0A9W6GRP9_9HYPH
Original site: A0A9W6GRP9_9HYPH 
ID   A0A9W6GRP9_9HYPH        Unreviewed;       861 AA.
AC   A0A9W6GRP9;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
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   Name=mgt {ECO:0000313|EMBL:GLI91847.1};
GN   ORFNames=LMG27198_08390 {ECO:0000313|EMBL:GLI91847.1};
OS   Methylocystis echinoides.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=29468 {ECO:0000313|EMBL:GLI91847.1, ECO:0000313|Proteomes:UP001144323};
RN   [1] {ECO:0000313|EMBL:GLI91847.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG27198 {ECO:0000313|EMBL:GLI91847.1};
RX   PubMed=37279153; DOI=10.1099/ijsem.0.005925;
RA   Kaise H., Sawadogo J.B., Alam M.S., Ueno C., Dianou D., Shinjo R.,
RA   Asakawa S.;
RT   "Methylocystis iwaonis sp. nov., a type II methane-oxidizing bacterium from
RT   surface soil of a rice paddy field in Japan, and emended description of the
RT   genus Methylocystis (ex Whittenbury et al. 1970) Bowman et al. 1993.";
RL   Int. J. Syst. Evol. Microbiol. 73:895-898(2023).
CC   -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC       {ECO:0000256|ARBA:ARBA00003954}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mg(2+)(out) + ATP + H2O = Mg(2+)(in) + ADP + phosphate + H(+);
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:ARBA00047295};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}.
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:GLI91847.1}.
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DR   EMBL; BSEC01000001; GLI91847.1; -; Genomic_DNA.
DR   RefSeq; WP_281800706.1; NZ_BSEC01000001.1.
DR   AlphaFoldDB; A0A9W6GRP9; -.
DR   Proteomes; UP001144323; 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   CDD; cd02077; P-type_ATPase_Mg; 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; 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; IPR059000; ATPase_P-type_domA.
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   NCBIfam; NF011702; PRK15122.1; 1.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR01836; MGATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:ARBA00022475};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001144323};
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        68..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        734..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        769..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        797..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..88
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   861 AA;  92751 MW;  AB3AE92D8032F8EE CRC64;
     MTLSKNQISR QALIRAAAAP ADAVLHDLDS SREGLAEDES ARRLRRFGPN RVAQDSGGGL
     LRELARHVFN PLNGLLLTLA AASFALSDQR SAIVISAIVV LSVLLAFVQE HRANNAAAEL
     RAMVRTHASV RRPGRAGDPF EEISLEELTP GDIVRLAAGD MIPADVRLIA TKDLFINQSA
     LTGESMPVEK FAAPAPGVEP MAAACLAFMG SNVLSGYGEA VVVATGAQTV FGQIGDTIVG
     AEEPTAFDES VKKFTLLMIA FMAVMAPATF FINGALKGDW LAAFLFAISV AVGLTPEMLP
     MIVTVNLAKG AMALAREKVI VKRLAAIQNF GAMDVLCTDK TGTLTQDRII LKRHLDIYGA
     DSERVLEFAY LNSHFQSGLR NLLDVAVLQH ADIAERLAPQ QVFTKIDEIP FDFERRRLSV
     VVEQEDGARL LICKGAVEEI FTVSSRYEAE SASGPLDPSH LDAAKQETAA LNADGFRVIA
     VAYKDVSRAQ QVFTAADETG LTLLGYIAFL DPPKDSAAGA IADLRKAGVS VKILTGDNEI
     VTRKVCRDVG LEIEGLALGA DVDAMDDDAL AACVSGVTVF AKLSPPQKAR VVSALRRGGH
     VVGYLGDGIN DGPALKAGDV GISVDTATDI ARESADIILL EKSLAVLNDG VLEGRKVFAN
     ILKYVRMGAS SNFGNMFSVL GASVFLPFLP MTPIQILTNS LLYDFSQTAI PTDNVDEEFL
     EEPRKWEIGG IARFMLYLGP VSSIFDYATF MLMLVVFDAW DKPQLFQTGW FVESLFTQTL
     VIHIIRTRRI PFIQSRASGA LILTTIIVCL IGAALPYSPL APVFGFTPLP PAYWPIVGLF
     LISYAILAHL AKTAYFERFE E
//
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