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Database: UniProt
Entry: A0A1J4TQK4_9BACT
LinkDB: A0A1J4TQK4_9BACT
Original site: A0A1J4TQK4_9BACT 
ID   A0A1J4TQK4_9BACT        Unreviewed;       835 AA.
AC   A0A1J4TQK4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=AUJ73_04680 {ECO:0000313|EMBL:OIO12957.1};
OS   Candidatus Gottesmanbacteria bacterium CG1_02_37_22.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1805209 {ECO:0000313|EMBL:OIO12957.1, ECO:0000313|Proteomes:UP000183120};
RN   [1] {ECO:0000313|EMBL:OIO12957.1, ECO:0000313|Proteomes:UP000183120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_37_22 {ECO:0000313|EMBL:OIO12957.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIO12957.1}.
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DR   EMBL; MNUY01000074; OIO12957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4TQK4; -.
DR   STRING; 1805209.AUJ73_04680; -.
DR   Proteomes; UP000183120; 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; 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: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        50..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        703..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        732..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        764..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        799..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..78
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  93994 MW;  E9E90AEDB46B8F2E CRC64;
     MAEISREANS LENNNDTREE PSEGLTSHEA RRRYRAYGAN EIVHAKKKGI FIAFLSKFGN
     PLVIILLFAS FVSALTGEWV NFVVIFAMIL FSVVIESYQE YQSEEAAEKL KHKVAVRVVV
     MRDGEKKEVL VSHVTIGDLV LLEIGDVVPA DAKVLSSKDF HLDESSLTGE SFPVEKGEKD
     EVWMGSSVVN GEAQVRVVRI GKNTQIGQIA DKLTHKKPET DFEKGIRKFG LLIMRITIIL
     VFFIFITNIF FKHDIFSSLL FALALAVGLT PELLPMIVTV NLSKGAMRMA KKGVIVKHLP
     AIQNFGSMEI LCTDKTGTIT ENKIRLERYE NAKGGEDRKV LSLAYLNSSY QTNMKSPLDD
     AILAHREVED ASFQKTDEIP FDFLRKRLSV VLRKDGRDLL ITKGAPEGMW DITRHFKEDG
     KVVHLDEYKL AKLKERFVKL SSEGFRVLTI AYKINNVTKD TYEQSDEKDL IFLGFTAFLD
     PPKKEVKEVL ASLNRHGVDL KILTGDNEQV TAKVCKDLGI PVSGLVLGKD ILHVSDEALI
     PLVLKANIFA RLTPDEKERI IKALKKTGKV VGFMGDGVND AISLRAADVG ISVNNAVDVA
     KESADIILVT KSLLVLKEGI KEGRQTFANT MKYIYMGSGS NFGNMFSVSV ASLFLPFLPM
     LPIQILLNNL IYDLSQLTLP ADRVDSADIE KPQKWDMGFI KKFIYTFGPI SSFFDMVTFL
     SLLYIFKASV PFFRTGWFME SLITQIVIIL MVRTRKVPFW KSKPSRIVVL GVLIAILSGI
     IITQSRLGQI FEFVSLSPIY WIFLLLIITF YIIFVELAKA WFYRKADLHI YKTHH
//
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