ATMA_ECOLI
ID ATMA_ECOLI Reviewed; 898 AA.
AC P0ABB8; P39168; Q2M665;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
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; Synonyms=corB, mgt; OrderedLocusNames=b4242, JW4201;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 301-317.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA Mori H., Ishihama A., Utsumi R.;
RT "Identification and molecular characterization of the Mg2+ stimulon of
RT Escherichia coli.";
RL J. Bacteriol. 185:3696-3702(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP ACTIVITY REGULATION, AND INTERACTION WITH MGTS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28512220; DOI=10.1073/pnas.1703415114;
RA Wang H., Yin X., Wu Orr M., Dambach M., Curtis R., Storz G.;
RT "Increasing intracellular magnesium levels with the 31-amino acid MgtS
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:5689-5694(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 383-545.
RX PubMed=19923713; DOI=10.1107/s090744490903306x;
RA Hakansson K.O.;
RT "The structure of Mg-ATPase nucleotide-binding domain at 1.6 A resolution
RT reveals a unique ATP-binding motif.";
RL Acta Crystallogr. D 65:1181-1186(2009).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000250|UniProtKB:P36640}.
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 -!- ACTIVITY REGULATION: Upon Mg(2+) depletion, MgtA is stabilized by
CC interaction with MgtS. {ECO:0000269|PubMed:28512220}.
CC -!- SUBUNIT: Interacts with MgtS. {ECO:0000269|PubMed:28512220}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by low levels of proline and by osmotic shock. The
CC leader of mgtA mRNA functions as a riboswitch, favoring transcription
CC under low Mg(2+) conditions. Under limiting proline levels the MgtL
CC peptide encoded within the mgtA leader cannot be translated, thereby
CC favoring the transcription of the mgtA ORF. Induction by osmotic shock
CC also depends on translational regulation by MgtL (Probable). Induced by
CC low extracellular levels of Mg(2+) via the PhoQ/PhoP two-component
CC regulatory system. {ECO:0000269|PubMed:12813061, 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; U14003; AAA97139.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77199.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78241.1; -; Genomic_DNA.
DR PIR; E65236; E65236.
DR RefSeq; NP_418663.1; NC_000913.3.
DR RefSeq; WP_000471889.1; NZ_LN832404.1.
DR PDB; 3GWI; X-ray; 1.60 A; A=383-545.
DR PDBsum; 3GWI; -.
DR AlphaFoldDB; P0ABB8; -.
DR SMR; P0ABB8; -.
DR BioGRID; 4261853; 110.
DR DIP; DIP-48092N; -.
DR IntAct; P0ABB8; 2.
DR STRING; 511145.b4242; -.
DR jPOST; P0ABB8; -.
DR PaxDb; P0ABB8; -.
DR PRIDE; P0ABB8; -.
DR EnsemblBacteria; AAC77199; AAC77199; b4242.
DR EnsemblBacteria; BAE78241; BAE78241; BAE78241.
DR GeneID; 948778; -.
DR KEGG; ecj:JW4201; -.
DR KEGG; eco:b4242; -.
DR PATRIC; fig|1411691.4.peg.2459; -.
DR EchoBASE; EB2416; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_6_3_6; -.
DR InParanoid; P0ABB8; -.
DR OMA; GVHRMAK; -.
DR PhylomeDB; P0ABB8; -.
DR BioCyc; EcoCyc:MGTA-MON; -.
DR BRENDA; 7.2.2.14; 2026.
DR EvolutionaryTrace; P0ABB8; -.
DR PRO; PR:P0ABB8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; TAS:EcoCyc.
DR GO; GO:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0071286; P:cellular response to magnesium ion; IEP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..898
FT /note="Magnesium-transporting ATPase, P-type 1"
FT /id="PRO_0000046182"
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"
FT CONFLICT 301..317
FT /note="PVVLLINGYTKGDWWEA -> AGGAVNQWLHQRRLVGS (in Ref. 1;
FT AAA97139)"
FT /evidence="ECO:0000305"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:3GWI"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 451..469
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 492..507
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 511..521
FT /evidence="ECO:0007829|PDB:3GWI"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:3GWI"
FT STRAND 534..544
FT /evidence="ECO:0007829|PDB:3GWI"
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
