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Database: UniProt
Entry: R2T3Y1_9ENTE
LinkDB: R2T3Y1_9ENTE
Original site: R2T3Y1_9ENTE 
ID   R2T3Y1_9ENTE            Unreviewed;       886 AA.
AC   R2T3Y1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=UAW_00864 {ECO:0000313|EMBL:EOH99711.1};
OS   Enterococcus haemoperoxidus ATCC BAA-382.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH99711.1, ECO:0000313|Proteomes:UP000013858};
RN   [1] {ECO:0000313|EMBL:EOH99711.1, ECO:0000313|Proteomes:UP000013858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH99711.1,
RC   ECO:0000313|Proteomes:UP000013858};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL   Submitted (FEB-2013) 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:EOH99711.1}.
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DR   EMBL; AJAR01000010; EOH99711.1; -; Genomic_DNA.
DR   RefSeq; WP_010761073.1; NZ_KE136479.1.
DR   AlphaFoldDB; R2T3Y1; -.
DR   STRING; 155618.RV06_GL002052; -.
DR   PATRIC; fig|1158608.3.peg.844; -.
DR   eggNOG; COG0474; Bacteria.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000013858; 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; 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        69..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        680..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        856..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..90
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   886 AA;  98476 MW;  244623247A23138A CRC64;
     MDKRAVLNKN NNQSYEYFAR NSAENILTFF NSSRMGLTHQ QAVLSREEFG ENIITHGKKT
     PLFVEIIKAY FTPFTIVLIT LAIISFITDY VIAPPADRDL IGVLIIVAMV LISGTMTLIQ
     SVKSNQAAEK LNNMVKITAT VVRRKKQVEL PIEEIVCGDI VKLSAGDMIP ADIRLTKTKD
     LFISQSAMTG ESYPVEKRAD YKLKVNSVET EYENIVFMGS NVISGSAEGI VVSVGDDTLF
     GKVAQDVSDK NPQTNFEVGI SKTSWLLIRF MLVMAPAVFL INGLTKGDWF EAFLFGLSVA
     VGLTPEMLPM IVTTNLVKGA SSMAKKGTII KNLNAIQNFG AIDVLCTDKT GTLTQDKIIL
     EYHLDCDGKE DSRVLRHAFF NSYYQTGLKN LMDVAIIDAA NDELSIDSSK YKKVDEIPFD
     FKRRRMSVVI EDTSGKTQMI TKGAVEEMLE ISSFVDYQGT VRPLTKTLKT EILKTVEELN
     EDGLRVLAVS QKTNPATVDE FSVSDENEMV LIGYLAFLDP PKETTKAALE ALKKHGVGVK
     VLTGDNALVT KSVCKQVGLA NEELITGNEI ARMNDFELKM VAEKYNIFVK LTPQQKTRIV
     QVLREAGHTV GFMGDGINDA PAMKEADVGI SVDTAVDIAK ESADVILLEK DLMVLERGLL
     AGRTTFGNIM KYVKMTASSN FGNMFSVVVA SIFLPFLPML PLQLLFLNLI YDISCMSIPW
     DHVDDEYLEQ PKKWNASKIG SFMKWLGPTS SVFDITTYLL MYFIICPQLV GGNYHDLDPA
     QQATFIAIFH AGWFIESLWS QTLVIHTLRT PKIPFIQSRA SFILTTITTL GIAVGTILPF
     TSFGENLGLA ELPLHYFAWL GLTIFAYLFL VMIVKKFYVK RFGELL
//
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