ATMA_SALT1
ID ATMA_SALT1 Reviewed; 902 AA.
AC D0ZTB2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=STM14_5349;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP INDUCTION.
RX PubMed=20813261; DOI=10.1016/j.cell.2010.07.046;
RA Park S.Y., Cromie M.J., Lee E.J., Groisman E.A.;
RT "A bacterial mRNA leader that employs different mechanisms to sense
RT disparate intracellular signals.";
RL Cell 142:737-748(2010).
CC -!- FUNCTION: Mediates magnesium influx to the cytosol. {ECO:0000305}.
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:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: By low extracellular levels of Mg(2+) and by low levels of
CC proline; induction is higher in the absence of both. Also by osmotic
CC shock (0.3 M NaCl). The leader of mgtA mRNA functions as a riboswitch;
CC at low Mg(2+) stem loop 'C' forms which favors transcription of the
CC full-length mgtA mRNA. Under limiting proline levels the 17 residue,
CC proline-rich MgtL peptide encoded within the mgtA leader is unable to
CC be fully translated, and the same stem loop 'C' is able to fold, again
CC favoring transcription of the full mgtA mRNA. Osmotic shock induction
CC also depends on MgtL translation. {ECO:0000269|PubMed:20813261}.
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; CP001363; ACY91682.1; -; Genomic_DNA.
DR RefSeq; WP_001738655.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZTB2; -.
DR SMR; D0ZTB2; -.
DR EnsemblBacteria; ACY91682; ACY91682; STM14_5349.
DR KEGG; seo:STM14_5349; -.
DR PATRIC; fig|588858.6.peg.4845; -.
DR HOGENOM; CLU_002360_6_3_6; -.
DR OMA; GVHRMAK; -.
DR BioCyc; SENT588858:STM14_RS23360-MON; -.
DR BRENDA; 7.2.2.14; 2169.
DR Proteomes; UP000002695; 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 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..902
FT /note="Magnesium-transporting ATPase, P-type 1"
FT /id="PRO_0000403461"
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
