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}.
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; 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
//