ID A0A1J0A8H9_9ENTE Unreviewed; 880 AA.
AC A0A1J0A8H9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BHY08_04405 {ECO:0000313|EMBL:APB32217.1};
OS Vagococcus teuberi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=519472 {ECO:0000313|EMBL:APB32217.1, ECO:0000313|Proteomes:UP000191200};
RN [1] {ECO:0000313|EMBL:APB32217.1, ECO:0000313|Proteomes:UP000191200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21459 {ECO:0000313|EMBL:APB32217.1,
RC ECO:0000313|Proteomes:UP000191200};
RA Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA Stevens M.J., Meile L.;
RT "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT fene.";
RL Submitted (SEP-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; CP017267; APB32217.1; -; Genomic_DNA.
DR RefSeq; WP_071457826.1; NZ_CP017267.1.
DR AlphaFoldDB; A0A1J0A8H9; -.
DR STRING; 519472.BHY08_04405; -.
DR KEGG; vte:BHY08_04405; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000191200; Chromosome.
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; 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:ARBA00022519};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191200};
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 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 746..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..84
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 880 AA; 97208 MW; 9F28A3614E483098 CRC64;
MEKKEVANYK FFAQTSIDKL FSTFKTSLSG INNNEAEVLR DEYGENVISH KKKTPFIIEV
LKAYFTPFTT VLLALAIISF ITDYVIVPAD EKDLTGVLII VAMVLLSGTM TLVQSVKSNN
AAEKLSNMVK VTATVLRKGE EVELPIEEIV CGDIIKLSAG DMLPADVRLI RTKDLFVSQA
AMTGESYPVE KKDTFTMRNK DTETDYENIA FMGSNVVSGS AIGLVIAVGN GTLFGQIAKD
VSEKHTITSF DVGISKTSWL LIRFMLVMAP TVFLINGLTK GDWLEAFLFG LSVAVGLTPE
MLPMIVTTNL VKGASTMAKK GTIIKNLNSI QNFGAIDVLC TDKTGTLTQD KIILEYHLDV
DGKEDDRVLR HAFFNSYYQT GLKNLMDKAI IESAEEELNM NVNAYKKVDE IPFDFQRRRM
SVVIEDAFGK TQMITKGAVE EMLDVSSYVD YRGSVVPLTE EIKSTILKTV DELNEDGLRV
IAVAQKTNPS VVGEFSVKDE SDMVLIGYLA FLDPPKETTK DALKALKEHG VGVKVLTGDN
ALVTKSVCKQ VGLEDEELIT GSEISHMNDV ELKVIAEKYN IFVKLTPSQK TRLVKVLRDA
GHTVGFMGDG INDAPAMKEA DVGISVDTAV DIAKESADVI LLEKDLMVLE RGILAGRTTF
GNIMKYVKMT ASSNFGNMFS VVVASIFLPF LPMLPIQLLF LNLIYDISCM SIPWDNMDAD
YLEEPKKWDA SRIGSFMKWL GPTSSVFDIT TYALMYFVIC PAVVGGSYHT LGAEQQALFI
AVFHAGWFVE SLWSQTLVIH TLRTPKLPFI QSRASFILTT ITSIGIAIGS FLPFTAFGQD
LGLMPLPGQY WIYLALTIVA YLMLVMVVKK IYVNRFGELL
//
