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Database: UniProt
Entry: A0A1H7J3U2_9ACTN
LinkDB: A0A1H7J3U2_9ACTN
Original site: A0A1H7J3U2_9ACTN 
ID   A0A1H7J3U2_9ACTN        Unreviewed;       911 AA.
AC   A0A1H7J3U2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-JAN-2026, 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=SAMN05660976_01014 {ECO:0000313|EMBL:SEK69399.1};
OS   Nonomuraea pusilla.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46177 {ECO:0000313|EMBL:SEK69399.1, ECO:0000313|Proteomes:UP000198953};
RN   [1] {ECO:0000313|EMBL:SEK69399.1, ECO:0000313|Proteomes:UP000198953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43357 {ECO:0000313|EMBL:SEK69399.1,
RC   ECO:0000313|Proteomes:UP000198953};
RA   de Groot N.N.;
RL   Submitted (OCT-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 = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00049360};
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}.
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DR   EMBL; FOBF01000002; SEK69399.1; -; Genomic_DNA.
DR   RefSeq; WP_091098618.1; NZ_FOBF01000002.1.
DR   AlphaFoldDB; A0A1H7J3U2; -.
DR   STRING; 46177.SAMN05660976_01014; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000198953; 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; 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   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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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:UP000198953};
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        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        741..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        770..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        829..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..95
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   911 AA;  96920 MW;  A779C698AC602FC8 CRC64;
     MSTPGTSGGT QPATGAGGVE ITAAAALTAD DVLVRLRTSP GGLPEDEARR RLRTVGPNAL
     RTHRARGLAV LARQLRSPLL VLLAVTAVAS FFVGERADAL IIGVILAASV GLGFFNEYRA
     ERAAEALHSQ IRHRCLVLRD GRPRLLDVTD LVPGDVVELR LGDVVPADLR LLAVADLECE
     ESVLTGESLP VAKSPEPVPE GESLAELASC ALMGTVVHAG SGTGVVVATG GAAEFGRIAL
     QLGERHPETE FQVGLRKFSL LLVRVAAALT VSIFAINVVL DRPFIDALLF SLAIAVGISP
     QLLPAVVSTG LAAGTRRLAR HKVLVKRLVC IEDLGDIDVL FTDKTGTLTE GRITFARALG
     PDGRPSDETL ELGLLCNEAV AAGDEDAGPG PASGMLTGPA LDVALWEAPG AGTLRPELER
     CRRLDILPFD HQRRAASVMV RREDGGTTLV TKGAPEYVLA RCPAAGGQAR SMLEAEFAAG
     NRVVAVATRQ ITEGERQGAL SPADERDLTF RGLLVFLDPP KPSAPHALER LTALGVTVKV
     LTGDNATVAA KLCADLGLPP GRVLTGHDVD AAGDDELAGL IEQATVFARV SPEHKARIVR
     TQRRAGLDVA FLGDGVNDAI ALHAADVGIS VETATDVAKD AADVLLLEKN LDILADGVVQ
     GRRIFANTMK YVLMGTSSNF GNMFSAAGAS AFLPFLPMLP SQILLNNLLY DTSQLAIPTD
     TVDAEQVARP TRWDVRLIRR FMLFFGPISS VFDFVTFGIM LWVFHAGPPL FRTGWFVESL
     ATQTLVIFAI RTRRIPFFRS RPSLALLLAT LTVVTVGAVL PLTPLAPLLG FQLLPAPFFL
     ALGLMVVAYL GLIEAGKRWF FRAAPPSAAG RERTPAHRTH RRAHRFTTAG ALRHGRRRAG
     FTAGRGRGRR R
//
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