ATMA_ECO57
ID ATMA_ECO57 Reviewed; 898 AA.
AC P0ABB9; P39168;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1;
DE EC=7.2.2.14 {ECO:0000250|UniProtKB:P36640};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1;
GN Name=mgtA; OrderedLocusNames=Z5853, ECs5219;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol. {ECO:0000250}.
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:0000250|UniProtKB:P36640};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By low extracellular levels of Mg(2+), proline and by
CC osmotic shock. The leader of mgtA mRNA functions as a riboswitch,
CC favoring transcription under low Mg(2+). Under limiting proline levels
CC the MgtL peptide encoded within the mgtA leader is unable to be
CC translated, also favoring transcription of full mgtA mRNA. Osmotic
CC shock induction also depends on MgtL translation (Probable).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG59440.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38642.1; -; Genomic_DNA.
DR PIR; C91281; C91281.
DR RefSeq; NP_313246.1; NC_002695.1.
DR RefSeq; WP_000471889.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ABB9; -.
DR SMR; P0ABB9; -.
DR STRING; 155864.EDL933_5592; -.
DR EnsemblBacteria; AAG59440; AAG59440; Z5853.
DR EnsemblBacteria; BAB38642; BAB38642; ECs_5219.
DR GeneID; 913855; -.
DR KEGG; ece:Z5853; -.
DR KEGG; ecs:ECs_5219; -.
DR PATRIC; fig|386585.9.peg.5457; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_6; -.
DR OMA; GVHRMAK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR01836; MGATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01524; ATPase-IIIB_Mg; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..898
FT /note="Magnesium-transporting ATPase, P-type 1"
FT /id="PRO_0000046183"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..335
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..715
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..724
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..744
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..790
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..818
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 819..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..851
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..866
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..886
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 373
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 641
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 734
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 898 AA; 99466 MW; 2B097D67E3FFA956 CRC64;
MFKEIFTRLI RHLPSRLVHR DPLPGAQQTV NTVVPPSLSA 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
