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Database: UniProt
Entry: A0A242AVY6_9ENTE
LinkDB: A0A242AVY6_9ENTE
Original site: A0A242AVY6_9ENTE 
ID   A0A242AVY6_9ENTE        Unreviewed;       886 AA.
AC   A0A242AVY6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=A5821_000697 {ECO:0000313|EMBL:OTN84768.1};
OS   Enterococcus sp. 7F3_DIV0205.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834189 {ECO:0000313|EMBL:OTN84768.1, ECO:0000313|Proteomes:UP000194948};
RN   [1] {ECO:0000313|EMBL:OTN84768.1, ECO:0000313|Proteomes:UP000194948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7F3_DIV0205 {ECO:0000313|EMBL:OTN84768.1,
RC   ECO:0000313|Proteomes:UP000194948};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 7F3_DIV0205.";
RL   Submitted (MAY-2017) 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:OTN84768.1}.
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DR   EMBL; NGKX01000001; OTN84768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A242AVY6; -.
DR   STRING; 1834189.A5821_000697; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000194948; 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; 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   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;  98122 MW;  0E46C0428F348206 CRC64;
     MEKRVLETKQ SNQSYEYFAR NSIENIITYF KSSKGGLTHQ QAVLSREEYG ENIITHGKKT
     PLFLEVIKAY FTPFTIVLLT LAIISFITDY VIAAPADRDL VGVLIILAMV LISGTMTLIQ
     SVKSNQAAEK LNNLVKVTAT VVRRKKTVEL PIEEIVCGDI VKLSAGDMIP ADIRLTKTKD
     LFVSQSAMTG ESYPVEKRAD YKLKVNSVET EYENIVFMGS NVISGSAEGI VVSVGDGTLF
     GKVAQDVSDK NPQTNFEVGI SKTSWLLIRF MLVMAPAVFL INGLTKGDWF EAFLFGLSVA
     VGLTPEMLPM IVTTNLVKGA SSMAKKGTII KNLNAIQNFG AIDILCTDKT GTLTQDKIIL
     EYHLDCDGKE DSRVLRHAFF NSYYQTGLKN LMDVAIIDAA KSELSIDPSE YRKVDEIPFD
     FKRRRMSVVI EDTSGKTQMI TKGAVEEMLE ISGYVDYQGT VTPLTEELKS EILKTVEELN
     EDGLRVLAVS QKTNPATVDE FSVSDENEMV LIGYLAFLDP PKETTKAALE ALKNHGVGVK
     VLTGDNALVT KSVCKQVGLA NEELITGNEI TRMNDFELKT IAEKYNIFVK LTPQQKTRIV
     QVLREAGHTV GFMGDGINDA PAMKEADVGI SVDTAVDIAK ESADVILLEK DLMVLERGLL
     AGRTTFGNIM KYVKMTASSN FGNMFSVVVA SIFLPFLPML PLQLLFLNLI YDISCMSIPW
     DHVDDEYLEQ PKKWDASKIG SFMTWLGPTS SVFDITTYLL MYFVICPQLV GGNYHDLAPA
     QQATFIAIFH AGWFVESLWS QTLVIHTLRT PKMPFLQSRA SFILTTITSL GIAVGTILPF
     TGFGQSLGLA ELPLNYFAWL GLTIVSYLIL VMIVKKFYVR RFGELL
//
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