ID S3J8L4_9ENTR Unreviewed; 897 AA.
AC S3J8L4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF0201_02792 {ECO:0000313|EMBL:EPF16432.1};
OS Cedecea davisae DSM 4568.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cedecea.
OX NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF16432.1, ECO:0000313|Proteomes:UP000014585};
RN [1] {ECO:0000313|EMBL:EPF16432.1, ECO:0000313|Proteomes:UP000014585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF16432.1,
RC ECO:0000313|Proteomes:UP000014585};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2013) 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:EPF16432.1}.
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DR EMBL; ATDT01000023; EPF16432.1; -; Genomic_DNA.
DR RefSeq; WP_016537087.1; NZ_KE161030.1.
DR AlphaFoldDB; S3J8L4; -.
DR STRING; 566551.HMPREF0201_02792; -.
DR PATRIC; fig|566551.4.peg.2560; -.
DR HOGENOM; CLU_002360_6_3_6; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000014585; 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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..93
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 897 AA; 98929 MW; B2420670652C619E CRC64;
MTVQTKNRNK KSTLSMRAAQ EAKNGIAETL VNLNTTREGL QEAHASARLE RDGLNEVAHD
KPPHALLQLL MAFNNPFIYV LAILAGISFF TDYWLPTSHG EEGDLTTVII IGTMVALSGL
VRFWQEHRSA KSAEALKAMV RTTATVVRRE HAGQKGTPRE IPMRELVVGD IVQLYAGDMI
PADVRLIESR DLFISQAVLT GEALPIEKYD TLGDVAQKSA HDKADESENL LDLPNICFMG
TNVVSGTALA VVVATGPRTY FGSLAKAIVG TRAQTAFDRG VNSVSWLLIR FMLVMVPVVF
LINGLMKGEW WDALLFALAV AVGLTPEMLP MIVSANLAKG AVAMAKRKVV VKRLNAIQNL
GAMDVLCTDK TGTLTQDKII LEHHVDTHGQ KNESVLALAW LNSHHQSGIK NLMDQAVIYF
SENEPGFVKP QGFSKVDEMP FDFVRRRLSI VVKDAQSNHL LVCKGAVEEM LSIATHMEEN
GKVIALDQPR RDAMLAMTND YNKDGFRVLV VATRDIPKAE AKKQYGADDE HDLIIRGFLT
FLDPPKESAG PAIAALMDIG VAVKVLTGDN AIVTTRICRQ VGLEPGEPVL GPQIEQLSDA
SLQQLVEERT VFAKLTPLQK SRVLKALQAN GHTVGFLGDG INDAPALRDA DVGISVDSGT
DIAKESADII LLEKSLMVLE EGVIKGRETF GNIMKYLNMT ASSNFGNVFS VLVASAFIPF
LPMLAIQLLL QNLMYDISQL ALPWDKTDKE FLSKPRKWDA KNIGRFMVWI GPTSSIFDMT
TFALMWFVFS ANSEHMQTLF QSGWFVEGLL SQTLVVHMLR TQKIPFIQST AAWPVMMMTG
LVMAVGIYVP FSPLGPLVGL QALPWQYFPW LVGTLLAYCC VAQGMKTFYM RRFKQWH
//
