ATMA_SALTY
ID ATMA_SALTY Reviewed; 902 AA.
AC P36640;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Magnesium-transporting ATPase, P-type 1;
DE EC=7.2.2.14 {ECO:0000269|PubMed:2670893};
DE AltName: Full=Mg(2+) transport ATPase, P-type 1;
GN Name=mgtA; OrderedLocusNames=STM4456;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=7751273; DOI=10.1128/jb.177.10.2654-2662.1995;
RA Tao T., Snavely M.D., Farr S.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: mgtA encodes a P-type
RT ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-
RT type ATPase.";
RL J. Bacteriol. 177:2654-2662(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION.
RX PubMed=2548998; DOI=10.1128/jb.171.9.4742-4751.1989;
RA Hmiel S.P., Snavely M.D., Florer J.B., Maguire M.E., Miller C.G.;
RT "Magnesium transport in Salmonella typhimurium: genetic characterization
RT and cloning of three magnesium transport loci.";
RL J. Bacteriol. 171:4742-4751(1989).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=2548999; DOI=10.1128/jb.171.9.4752-4760.1989;
RA Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: expression of cloned genes
RT for three distinct Mg2+ transport systems.";
RL J. Bacteriol. 171:4752-4760(1989).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2670893; DOI=10.1128/jb.171.9.4761-4766.1989;
RA Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: (28)Mg2+ transport by the
RT CorA, MgtA, and MgtB systems.";
RL J. Bacteriol. 171:4761-4766(1989).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC {ECO:0000269|PubMed:2548998, ECO:0000269|PubMed:2670893}.
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:0000269|PubMed:2670893};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for magnesium ions (at 20 degrees Celsius)
CC {ECO:0000269|PubMed:2670893};
CC KM=29 uM for magnesium ions (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:2670893};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2548999};
CC Multi-pass membrane protein {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+). {ECO:0000269|PubMed:7751273,
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; U07843; AAA68988.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23275.1; -; Genomic_DNA.
DR PIR; B57147; B57147.
DR RefSeq; NP_463316.1; NC_003197.2.
DR RefSeq; WP_001738655.1; NC_003197.2.
DR AlphaFoldDB; P36640; -.
DR SMR; P36640; -.
DR STRING; 99287.STM4456; -.
DR TCDB; 3.A.3.4.1; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P36640; -.
DR EnsemblBacteria; AAL23275; AAL23275; STM4456.
DR GeneID; 1255982; -.
DR KEGG; stm:STM4456; -.
DR PATRIC; fig|99287.12.peg.4689; -.
DR HOGENOM; CLU_002360_6_3_6; -.
DR OMA; GVHRMAK; -.
DR PhylomeDB; P36640; -.
DR BioCyc; SENT99287:STM4456-MON; -.
DR Proteomes; UP000001014; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..902
FT /note="Magnesium-transporting ATPase, P-type 1"
FT /id="PRO_0000046184"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..339
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..719
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..728
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..748
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..794
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..822
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..855
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..870
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 871..890
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 377
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 645
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 649
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 713
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 BINDING 742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 902 AA; 99783 MW; 3D2712E9A074C957 CRC64;
MLKIITRQLF ARLNRHLPYR LVHRDPLPGA QTAVNATIPP SLSERCLKVA AMEQETLWRV
FDTHPEGLNA AEVTRAREKH GENRLPAQKP SPWWVHLWVC YRNPFNILLT ILGGISYATE
DLFAAGVIAL MVGISTLLNF VQEARSTKAA DALKAMVSNT ATVLRVINEN GENAWLELPI
DQLVPGDIIK LAAGDMIPAD LRIIQARDLF VAQASLTGES LPVEKVAATR EPRQNNPLEC
DTLCFMGTNV VSGTAQAVVM ATGAGTWFGQ LAGRVSEQDN EQNAFQKGIS RVSMLLIRFM
LVMAPVVLII NGYTKGDWWE AALFALSVAV GLTPEMLPMI VTSTLARGAV KLSKQKVIVK
HLDAIQNFGA MDILCTDKTG TLTQDKIVLE NHTDISGKPS EHVLHCAWLN SHYQTGLKNL
LDTAVLEGVD ETAARQLSGR WQKIDEIPFD FERRRMSVVV AEDSNVHQLV CKGALQEILN
VCTQVRHNGD IVPLDDNMLR RVKRVTDTLN RQGLRVVAVA TKYLPAREGD YQRIDESDLI
LEGYIAFLDP PKETTAPALK ALKASGITVK ILTGDSELVA AKVCHEVGLD AGDVIIGSDI
EGLSDDALAA LAARTTLFAR LTPMHKERIV TLLKREGHVV GFMGDGINDA PALRAADIGI
SVDGAVDIAR EAADIILLEK SLMVLEEGVI EGRRTFSNML KYIKMTASSN FGNVFSVLVA
SAFLPFLPML PLHLLIQNLL YDVSQVAIPF DNVDEEQIQK PQRWNPADLG RFMVFFGPIS
SIFDILTFCL MWWVFHANTP ETQTLFQSGW FVVGLLSQTL IVHMIRTRRL PFIQSRAAWP
LMAMTLLVMV VGVSLPFSPL ASYLQLQALP LSYFPWLIAI LVGYMTLTQL VKGFYSRRYG
WQ
