ID A0A0P0FJK0_9BACT Unreviewed; 872 AA.
AC A0A0P0FJK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 Name=mgtA {ECO:0000313|EMBL:ALJ56990.1};
GN ORFNames=AMD24_00833 {ECO:0000313|EMBL:ALJ56990.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56990.1, ECO:0000313|Proteomes:UP000062177};
RN [1] {ECO:0000313|EMBL:ALJ56990.1, ECO:0000313|Proteomes:UP000062177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56990.1,
RC ECO:0000313|Proteomes:UP000062177};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
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; CP012665; ALJ56990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0FJK0; -.
DR STRING; 1704307.AMD24_00833; -.
DR KEGG; xii:AMD24_00833; -.
DR PATRIC; fig|1704307.3.peg.923; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000062177; 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 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 Hydrolase {ECO:0000313|EMBL:ALJ56990.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000062177};
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 73..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..89
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 872 AA; 96319 MW; A22BFF18BD133C0A CRC64;
MIPIQEQDPK FISANGEFLS LSPAGPHRKV YICKQGLTDK EVVARLKEWG PNQVTFTQKA
GWLSVFQRFK DPLVIQLLVI LTVAAAMGNF YSASVVFLMI LLSVGLSYVQ ERRSASAMSS
LQKKVRITAV VVRNGQEKEV GIEGIVPGDT VVLAAGSIVP ADLRILTAKD FFVSQSALTG
ESLPVEKSAK LGSLDARGTL ESPNACFMGS NVVSGSATAL VCATGRNTLL GKISERTVRR
KGATNFEKGL HNFSMLMVHV MVIMVAVVFL IVGATQHNWG EALLFGLSIA VGLTPEMLPV
ILTVCLSRGA LLMSKKKVIV RRLDAIQNFG AMDVLCTDKT GTLTQDHVVL ERYVDVTGRE
SEDVLRYAWM NSYYQTGLRN LLDKAVLAHT DLDVDHNCIK VDEIPFDFHR RRMSVIIGYG
GRHVLICKGA VEEMSAVCSR YQVDGEVYPL IPLVREDLWG EYRDLSTEGY RVVAVAYREF
SRSKTAFSKE DETGLILLGY ITFFDPPKDS SRSAIQALLE HGIAVKVLTG DNELVSRKIG
MDVGLQVGHV ATGPELAELS RDDFLQKVRE ASILARLSPI QKEQVVQTLK EQGHVVGFIG
DGINDVMAIK SADVGISVDT AVDVAKESAD IILLEKSLMV LEEGVVEGRK VFGNIVKYIK
TGASSNFGNM LSILGASCFL PFLPMTPIQI LVNNLLYDVA QIGIPLDNVD REYIEKPRKW
DITNIWKFMM FLGPVSSIFD FCTFFIMLYL FGCGAYQKVP LGVAVDSTST YLASFFHSAW
FVESLLTQTL VVYVIRTNRV PFLQSQPSVF LVLTTFTVMV VGVWLPYSPL AGFFGFVPLP
PIFWLWITGF MAAYVVLAHR IKTWFSTRFG YL
//
