ID D3GW42_ECO44 Unreviewed; 898 AA.
AC D3GW42;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:CBG37540.1};
GN OrderedLocusNames=EC042_4720 {ECO:0000313|EMBL:CBG37540.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG37540.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG37540.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
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; FN554766; CBG37540.1; -; Genomic_DNA.
DR RefSeq; WP_000471847.1; NC_017626.1.
DR AlphaFoldDB; D3GW42; -.
DR KEGG; elo:EC042_4720; -.
DR PATRIC; fig|216592.3.peg.4905; -.
DR HOGENOM; CLU_002360_6_3_6; -.
DR Proteomes; UP000001407; 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: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 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 Hydrolase {ECO:0000313|EMBL:CBG37540.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
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 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..117
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 898 AA; 99472 MW; B4F972DF06DF8641 CRC64;
MFKEIFTRFI RHLPSRLVHR DPLPGAQQTV NTAVPPSLSA HCLKMAVMPE EELWKTFDTH
PEGLNQAEVE SAREQHGENK LPAQQPSPWW VHLWVCYRNP FNILLTILGA ISYATEDLFA
AGVIALMVAI STLLNFIQEA RSTKAADALK AMVSNTATVL RVINDKGENG WLEIPIDQLV
PGDIIKLAAG DMIPADLRIL QARDLFVAQA SLTGESLPVE KAATTRQPEH SNPLECDTLC
FMGTTVVSGT AQAMVIATGA NTWFGQLAGR VSEQESEPNA FQQGISRVSM LLIRFMLVMA
PVVLLINGYT KGDWWEAALF ALSVAVGLTP EMLPMIVTST LARGAVKLSK QKVIVKHLDA
IQNFGAMDIL CTDKTGTLTQ DKIVLENHTD ISGKTSERVL HSAWLNSHYQ TGLKNLLDTA
VLEGTDEESA RSLASRWQKI DEIPFDFERR RMSVVVAENT EHHQLVCKGA LQEILNVCSQ
VRHNGEIVPL DDIMLRKIKR VTDTLNRQGL RVVAVATKYL PAREGDYQRA DESDLILEGY
IAFLDPPKET TAPALKALKA SGITVKILTG DSELVAAKVC HEVGLDAGEV VIGSDIETLS
DDELANLAQR TTLFARLTPM HKERIVTLLK REGHVVGFMG DGINDAPALR AADIGISVDG
AVDIAREAAD IILLEKSLMV LEEGVIEGRR TFANMLKYIK MTASSNFGNV FSVLVASAFL
PFLPMLPLHL LIQNLLYDVS QVAIPFDNVD DEQIQKPQRW NPADLGRFMI FFGPISSIFD
ILTFCLMWWV FHANTPETQT LFQSGWFVVG LLSQTLIVHM IRTRRVPFIQ SCASWPLMIM
TVIVMIVGIA LPFSPLASYL QLQALPLSYF PWLVAILAGY MTLTQLVKGF YSRRYGWQ
//
