ID A0A1H3WB24_9GAMM Unreviewed; 900 AA.
AC A0A1H3WB24;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02982996_00413 {ECO:0000313|EMBL:SDZ84275.1};
OS Lonsdalea quercina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Lonsdalea.
OX NCBI_TaxID=71657 {ECO:0000313|EMBL:SDZ84275.1, ECO:0000313|Proteomes:UP000187280};
RN [1] {ECO:0000313|EMBL:SDZ84275.1, ECO:0000313|Proteomes:UP000187280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29281 {ECO:0000313|EMBL:SDZ84275.1,
RC ECO:0000313|Proteomes:UP000187280};
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; FNQS01000001; SDZ84275.1; -; Genomic_DNA.
DR RefSeq; WP_074727785.1; NZ_FNQS01000001.1.
DR AlphaFoldDB; A0A1H3WB24; -.
DR STRING; 71657.SAMN02982996_00413; -.
DR eggNOG; COG0474; Bacteria.
DR Proteomes; UP000187280; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187280};
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 122..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..119
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 900 AA; 100875 MW; AC4720AE0BC77AFD CRC64;
MLFTRLTRQW LAQIRRHLPS RLFHRAPMPN GQANAIPERL ARQCHHYAWQ NEEALYQAFD
SHPEGLMPNE VRQARLTYGE NQIPGERAAP WWLHLWRCYR NPFNLLLTLL ALISYATEDL
TAALVIGLMV LISTLLHFIQ EARSGKAADT LKAMVSNTAT VLRCDEQTGR SEYQEIPMDQ
LVPGDIVKLA AGDMIPADLR VLQARDLFIS QASLTGESLP VEKVAQSRLA KNAPALESDT
LCFMGTNVIS GTAQAIVIGT GANTWFGQLA GRVTNQPGQE NAFQKGISRV SWLLIRFMMV
MTPIVLVING YTKGDWWEAA LFALSVAVGL TPEMLPMIVT STLAKGAVKL SRQKVIVKRL
DAIQNFGAMN ILCTDKTGTL TQDHIALESH TDAFGRCSQK VLRLAWLNSA HQTGLHNLLD
QAVLEGISDK EQRDVLSRWR KVDEIPFDFE RRRMSVVVAE NDREHRLICK GALEEMLSVC
SSIRLGEETM MLDEDRLLRI RHLTDDWNRQ GLRVVAVASK VVDAEPRDYS RVDESDLILE
GYIAFLDPPK ESTAPALKAL NNSGIAVKIL TGDSELVAAK VCRDVGIDCS QTLLGSHLDE
MTDEELSTQA ETTTLFARLT PMHKERIVRL LRAQGHVVGF MGDGINDAPA LRAADIGISV
DSAVDIAREA ADIILLEKSL MVLEQGVVEG RRTFANMLKY IKMTASSNFG NVFSVLIASA
FLPFLPMLPL HLLIQNLMYD ISQIAIPFDN VDDEQIRRPQ RWNAGDIGRF MVFFGPISSI
FDVATFALMW WVFQANTPEM QTLFQSGWFI EGLLSQTLIV HMIRTRKIPF FQSRPSWPLA
MMTLLIMAAG IALIFSPLAE FLELQSLPLS YFPWLIAILC GYMMLTQVMK GFFARRYGWQ
//
