ATMB_SALTY
ID ATMB_SALTY Reviewed; 908 AA.
AC P22036;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 174.
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=mgtB; OrderedLocusNames=STM3763;
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], DISRUPTION PHENOTYPE, AND PROBABLE
RP OPERON STRUCTURE.
RX PubMed=1824701; DOI=10.1016/s0021-9258(17)35246-8;
RA Snavely M.D., Miller C.G., Maguire M.E.;
RT "The mgtB Mg2+ transport locus of Salmonella typhimurium encodes a P-type
RT ATPase.";
RL J. Biol. Chem. 266:815-823(1991).
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, 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).
RN [6]
RP INDUCTION, AND OPERON STRUCTURE.
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 [7]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=8226755; DOI=10.1016/s0021-9258(18)41553-0;
RA Smith D.L., Tao T., Maguire M.E.;
RT "Membrane topology of a P-type ATPase. The MgtB magnesium transport protein
RT of Salmonella typhimurium.";
RL J. Biol. Chem. 268:22469-22479(1993).
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:0000250|UniProtKB:P36640};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for magnesium ions (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:2670893};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2548999,
CC ECO:0000269|PubMed:8226755}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8226755}.
CC -!- INDUCTION: Part of the mgtC/mgtB operon. Induced by low extracellular
CC levels of Mg(2+). {ECO:0000269|PubMed:7751273}.
CC -!- DISRUPTION PHENOTYPE: Decreases Mg(2+) influx.
CC {ECO:0000269|PubMed:1824701}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57715; AAA72084.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL22621.1; -; Genomic_DNA.
DR RefSeq; NP_462662.1; NC_003197.2.
DR RefSeq; WP_000131288.1; NC_003197.2.
DR AlphaFoldDB; P22036; -.
DR SMR; P22036; -.
DR STRING; 99287.STM3763; -.
DR PaxDb; P22036; -.
DR EnsemblBacteria; AAL22621; AAL22621; STM3763.
DR GeneID; 1255287; -.
DR KEGG; stm:STM3763; -.
DR PATRIC; fig|99287.12.peg.3981; -.
DR HOGENOM; CLU_002360_6_3_6; -.
DR OMA; GRVEVIC; -.
DR PhylomeDB; P22036; -.
DR BioCyc; SENT99287:STM3763-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; 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..908
FT /note="Magnesium-transporting ATPase, P-type 1"
FT /id="PRO_0000046185"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 81..101
FT /note="Helical; Name=1"
FT TOPO_DOM 102..113
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 114..134
FT /note="Helical; Name=2"
FT TOPO_DOM 135..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 294..314
FT /note="Helical; Name=3"
FT TOPO_DOM 315..323
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 324..341
FT /note="Helical; Name=4"
FT TOPO_DOM 342..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 705..724
FT /note="Helical; Name=5"
FT TOPO_DOM 725..733
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 734..753
FT /note="Helical; Name=6"
FT TOPO_DOM 754..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 776..799
FT /note="Helical; Name=7"
FT TOPO_DOM 800..808
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 809..827
FT /note="Helical; Name=8"
FT TOPO_DOM 828..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 841..860
FT /note="Helical; Name=9"
FT TOPO_DOM 861..875
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:8226755"
FT TRANSMEM 876..895
FT /note="Helical; Name=10"
FT TOPO_DOM 896..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8226755"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 650
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT CONFLICT 717
FT /note="G -> V (in Ref. 1; AAA72084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 100387 MW; 9C5451BC6E2BA7C2 CRC64;
MTDMNIENRK LNRPASENDK QHKKVFPIEA EAFHSPEETL ARLNSHRQGL TIEEASERLK
VYGRNEVAHE QVPPALIQLL QAFNNPFIYV LMALAGVSFI TDYWLPLRRG EETDLTGVLI
ILTMVSLSGL LRFWQEFRTN RAAQALKKMV RTTATVLRRG PGNIGAVQEE IPIEELVPGD
VVFLAAGDLV PADVRLLASR DLFISQSILS GESLPVEKYD VMADVAGKDS EQLPDKDKSL
LDLGNICLMG TNVTSGRAQA VVVATGSRTW FGSLAKSIVG TRTQTAFDRG VNSVSWLLIR
FMLIMVPVVL LINGFSKGDW VEASLFALAV AVGLTPEMLP MIVSSNLAKG AIAMSRRKVI
VKRLNAIQNF GAMDVLCTDK TGTLTQDNIF LEHHLDVSGV KSSRVLMLAW LNSSSQSGAR
NVMDRAILRF GEGRIAPSTK ARFIKRDELP FDFVRRRVSV LVEDAQHGDR CLICKGAVEE
MMMVATHLRE GDRVVALTET RRELLLAKTE DYNAQGFRVL LIATRKLDGS GNNPTLSVED
ETELTIEGML TFLDPPKESA GKAIAALRDN GVAVKVLTGD NPVVTARICL EVGIDTHDIL
TGTQVEAMSD AELASEVEKR AVFARLTPLQ KTRILQALQK NGHTVGFLGD GINDAPALRD
ADVGISVDSA ADIAKESSDI ILLEKDLMVL EEGVIKGRET FGNIIKYLNM TASSNFGNVF
SVLVASAFIP FLPMLAIHLL IQNLMYDISQ LSLPWDKMDK EFLRKPRKWD AKNIGRFMLW
IGPTSSIFDI TTFALMWYVF AANNVEAQAL FQSGWFIEGL LSQTLVVHML RTQKIPFIQS
RATLPVLLTT GLIMAIGIYI PFSPLGAMVG LEPLPLSYFP WLVATLLSYC LVAQGMKRFY
IKRFGQWF
