ID A0A1G7JNR4_9SPHI Unreviewed; 861 AA.
AC A0A1G7JNR4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05216464_11542 {ECO:0000313|EMBL:SDF26109.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDF26109.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDF26109.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDF26109.1,
RC ECO:0000313|Proteomes:UP000199072};
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 + 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}.
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DR EMBL; FNAI01000015; SDF26109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7JNR4; -.
DR STRING; 1391627.SAMN05216464_11542; -.
DR OrthoDB; 9770315at2; -.
DR Proteomes; UP000199072; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000199072};
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 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 826..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 861 AA; 93349 MW; 08DE7FAC7E41371A CRC64;
MPPQPHKLEK IKDTAPGSFW QLSEAEATSG LNCSNKGLSG QEAAVRRKQY GPNTIKANGR
SSGFFLFLSQ FKSPVTIMLI VAALLSAALG DVADTVIILT IVLISSLLGF WQERGAANAV
AELLKMVALH CAVLRDGKSR EISLDGVVPG DIVLLSAGDV IPADSLILDS QELFVDEAAF
TGETYPVEKN AGVLPADTPL AKRTNALFMG SHVISGKASV LVMKTGLQTE FGKISAGLQA
KVPETDFEKG IRKFGYMLME ITLVLVLVIF AINVFLHKPV LDSFLFSLAL AVGLTPQLLP
AIISVNLATG ARRMAKQKVI VKRLSSIQNF GSMDILCSDK TGTITAGKVK LKDTLDSNGQ
HSDKVLQYAW LNASLQQGFH NPIDEAICLG HKGAKPAYTV QTEIPYDFIR KRLTIQVKNG
KENFAVTKGA LRIVLDICTK IESGDGKVSS LVAGKEAILK QYEALSAAGF RTLGVAYKPG
DAAKDFTKAD EKDMVFLGFI TLFDPPKPGV AATLGKLNNL GVKLKIITGD NALVAKSLAL
QIGIEKPLIL TGAAMQKMSN AALSHQAPLT DIFAEVEPNQ KERIITLLKK AGHVVGFMGD
GINDAPALHT ADVGISVDTA VDVAKEAADI VLLSRDLDVL VDGIIEGRKT FANTMKYIFM
ATSANFGNMF SMAGASLFLK FLPLLPKQIL LTNLMTDFPE MTIATDRVDA LNIQSPQRWD
LGFIKRFMIT FGLLSSVFDY LTFGVLLLII HADEKVFQTG WFIESVISAT LIVLVVRTRL
PFFKSLPGKY LLVATVAVLL LVLALPLMPA ALWFGFTRLP LTYYSWMLLI IAAYMFSAEL
AKYWFYRKMN KAMSGGGLRK Q
//
