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Magnesium transporter MgtE

 MGTE_THET8              Reviewed;         450 AA.
Q5SMG8;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
28-MAR-2018, entry version 92.
RecName: Full=Magnesium transporter MgtE;
OrderedLocusNames=TTHA1060;
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
Thermus.
NCBI_TaxID=300852;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HB8 / ATCC 27634 / DSM 579;
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF GLU-59; ASP-226;
ASP-250; GLU-258; ASP-259; ARG-285; PHE-318; PRO-321; LEU-324;
ASN-329; ASN-332; GLN-333; GLU-359; ASN-424 AND ASP-432.
PubMed=19798051; DOI=10.1038/emboj.2009.288;
Hattori M., Iwase N., Furuya N., Tanaka Y., Tsukazaki T., Ishitani R.,
Maguire M.E., Ito K., Maturana A., Nureki O.;
"Mg(2+)-dependent gating of bacterial MgtE channel underlies Mg(2+)
homeostasis.";
EMBO J. 28:3602-3612(2009).
[3]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=17700703; DOI=10.1038/nature06093;
Hattori M., Tanaka Y., Fukai S., Ishitani R., Nureki O.;
"Crystal structure of the MgtE Mg(2+) transporter.";
Nature 448:1072-1076(2007).
-!- FUNCTION: Acts as a highly selective magnesium channel.
{ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:19798051}.
-!- ENZYME REGULATION: The channel activity is regulated by the
intracellular magnesium concentration. Under high-intracellular
magnesium conditions, binding of magnesium to the cytosolic
domains stabilizes the closed conformation of the channel. Under
low-intracellular magnesium conditions, the channel is in
equilibrium between the open and closed states.
{ECO:0000269|PubMed:19798051}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17700703}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15652583, EBI-15652583;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17700703};
Multi-pass membrane protein {ECO:0000269|PubMed:17700703}.
-!- SIMILARITY: Belongs to the SLC41A transporter family.
{ECO:0000305}.
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EMBL; AP008226; BAD70883.1; -; Genomic_DNA.
RefSeq; WP_011228410.1; NC_006461.1.
RefSeq; YP_144326.1; NC_006461.1.
PDB; 2YVX; X-ray; 3.50 A; A/B/C/D=1-450.
PDB; 2YVY; X-ray; 2.30 A; A=1-275.
PDB; 2YVZ; X-ray; 3.90 A; A/B=1-275.
PDB; 2ZY9; X-ray; 2.94 A; A/B=1-450.
PDB; 4U9L; X-ray; 2.30 A; A/B=271-449.
PDB; 4U9N; X-ray; 2.20 A; A/B=271-448.
PDB; 4WIB; X-ray; 3.20 A; A/B=271-448.
PDB; 5X9G; X-ray; 3.00 A; A/B/C/D=1-275.
PDB; 5X9H; X-ray; 3.60 A; A/B=1-450.
PDBsum; 2YVX; -.
PDBsum; 2YVY; -.
PDBsum; 2YVZ; -.
PDBsum; 2ZY9; -.
PDBsum; 4U9L; -.
PDBsum; 4U9N; -.
PDBsum; 4WIB; -.
PDBsum; 5X9G; -.
PDBsum; 5X9H; -.
ProteinModelPortal; Q5SMG8; -.
SMR; Q5SMG8; -.
DIP; DIP-60248N; -.
STRING; 300852.TTHA1060; -.
TCDB; 1.A.26.1.2; the mg(2+) transporter-e (mgte) family.
EnsemblBacteria; BAD70883; BAD70883; BAD70883.
GeneID; 3168925; -.
KEGG; ttj:TTHA1060; -.
PATRIC; fig|300852.9.peg.1040; -.
eggNOG; ENOG4105CJW; Bacteria.
eggNOG; COG2239; LUCA.
HOGENOM; HOG000280152; -.
KO; K06213; -.
OMA; TGPFITT; -.
PhylomeDB; Q5SMG8; -.
BioCyc; TTHE300852:G1GKC-1067-MONOMER; -.
BRENDA; 3.6.3.2; 2305.
EvolutionaryTrace; Q5SMG8; -.
Proteomes; UP000000532; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0015693; P:magnesium ion transport; NAS:UniProtKB.
Gene3D; 1.10.357.20; -; 1.
Gene3D; 1.25.60.10; -; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR006668; Mg_transptr_MgtE_intracell_dom.
InterPro; IPR038076; MgtE_N_sf.
InterPro; IPR038048; MgtE_transmem.
InterPro; IPR006669; MgtE_transporter.
InterPro; IPR006667; SLC41_membr_dom.
InterPro; IPR036739; SLC41_membr_dom_sf.
PANTHER; PTHR43773; PTHR43773; 1.
Pfam; PF00571; CBS; 2.
Pfam; PF01769; MgtE; 1.
Pfam; PF03448; MgtE_N; 1.
SMART; SM00116; CBS; 2.
SMART; SM00924; MgtE_N; 1.
SUPFAM; SSF161093; SSF161093; 1.
TIGRFAMs; TIGR00400; mgtE; 1.
PROSITE; PS51371; CBS; 2.
1: Evidence at protein level;
3D-structure; CBS domain; Cell membrane; Complete proteome; Magnesium;
Membrane; Metal-binding; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 450 Magnesium transporter MgtE.
/FTId=PRO_0000363889.
TOPO_DOM 1 277 Cytoplasmic.
TRANSMEM 278 305 Helical; Name=1.
INTRAMEM 306 320
TRANSMEM 321 344 Helical; Name=2.
TOPO_DOM 345 351 Cytoplasmic.
TRANSMEM 352 381 Helical; Name=3.
INTRAMEM 382 385
TRANSMEM 386 414 Helical; Name=4.
INTRAMEM 415 424
TRANSMEM 425 447 Helical; Name=5.
TOPO_DOM 448 450 Periplasmic.
DOMAIN 138 200 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 202 258 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
METAL 91 91 Magnesium 1.
METAL 95 95 Magnesium 2.
METAL 136 136 Magnesium 2; via carbonyl oxygen.
METAL 214 214 Magnesium 3.
METAL 216 216 Magnesium 4.
METAL 223 223 Magnesium 5; via carbonyl oxygen.
METAL 226 226 Magnesium 5.
METAL 247 247 Magnesium 1.
METAL 255 255 Magnesium 3.
METAL 258 258 Magnesium 3.
METAL 259 259 Magnesium 4.
METAL 418 418 Magnesium 4.
METAL 428 428 Magnesium 6; via carbonyl oxygen.
METAL 432 432 Magnesium 6.
MUTAGEN 59 59 E->A: Still possesses a slight channel
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 226 226 D->N: Abolishes the Mg(2+)-dependent
suppression of the Mg(2+) influx; when
associated with A-250.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 250 250 D->A: Abolishes the Mg(2+)-dependent
suppression of the Mg(2+) influx; when
associated with N-226.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 258 258 E->Q: Abolishes the Mg(2+)-dependent
suppression of the Mg(2+) influx.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 259 259 D->N: Abolishes the Mg(2+)-dependent
suppression of the Mg(2+) influx.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 285 285 R->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 318 318 F->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 321 321 P->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 324 324 L->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 329 329 N->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 332 332 N->A: Does not affect activity.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 333 333 Q->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 359 359 E->A: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
MUTAGEN 424 424 N->A: Does not affect activity.
{ECO:0000269|PubMed:19798051}.
MUTAGEN 432 432 D->A,N: Abolishes Mg(2+)-transport
activity. {ECO:0000269|PubMed:19798051}.
TURN 7 9 {ECO:0000244|PDB:2YVY}.
HELIX 10 15 {ECO:0000244|PDB:2YVY}.
HELIX 18 27 {ECO:0000244|PDB:2YVY}.
HELIX 30 35 {ECO:0000244|PDB:2YVY}.
HELIX 36 39 {ECO:0000244|PDB:2YVY}.
HELIX 42 51 {ECO:0000244|PDB:2YVY}.
HELIX 54 62 {ECO:0000244|PDB:2YVY}.
HELIX 66 75 {ECO:0000244|PDB:2YVY}.
HELIX 78 87 {ECO:0000244|PDB:2YVY}.
HELIX 90 103 {ECO:0000244|PDB:2YVY}.
HELIX 105 114 {ECO:0000244|PDB:2YVY}.
HELIX 117 128 {ECO:0000244|PDB:2YVY}.
HELIX 134 136 {ECO:0000244|PDB:2YVY}.
STRAND 142 145 {ECO:0000244|PDB:2ZY9}.
HELIX 151 161 {ECO:0000244|PDB:2YVY}.
TURN 162 164 {ECO:0000244|PDB:2YVY}.
STRAND 168 174 {ECO:0000244|PDB:2YVY}.
STRAND 179 185 {ECO:0000244|PDB:2YVY}.
HELIX 186 191 {ECO:0000244|PDB:2YVY}.
TURN 199 201 {ECO:0000244|PDB:2YVY}.
STRAND 202 205 {ECO:0000244|PDB:2YVY}.
STRAND 209 214 {ECO:0000244|PDB:2ZY9}.
HELIX 215 225 {ECO:0000244|PDB:2YVY}.
STRAND 228 233 {ECO:0000244|PDB:2YVY}.
STRAND 237 244 {ECO:0000244|PDB:2YVY}.
HELIX 245 251 {ECO:0000244|PDB:2YVY}.
STRAND 263 265 {ECO:0000244|PDB:2YVX}.
TURN 273 275 {ECO:0000244|PDB:4U9N}.
HELIX 278 296 {ECO:0000244|PDB:4U9N}.
HELIX 298 304 {ECO:0000244|PDB:4U9N}.
HELIX 307 312 {ECO:0000244|PDB:4U9N}.
HELIX 314 319 {ECO:0000244|PDB:4U9N}.
HELIX 320 343 {ECO:0000244|PDB:4U9N}.
HELIX 349 351 {ECO:0000244|PDB:4U9N}.
HELIX 352 381 {ECO:0000244|PDB:4U9N}.
HELIX 384 386 {ECO:0000244|PDB:4U9N}.
HELIX 387 414 {ECO:0000244|PDB:4U9N}.
HELIX 419 421 {ECO:0000244|PDB:4U9N}.
HELIX 423 447 {ECO:0000244|PDB:4U9N}.
SEQUENCE 450 AA; 50078 MW; 6F5930DCDDB90B05 CRC64;
MEEKLAVSLQ EALQEGDTRA LREVLEEIHP QDLLALWDEL KGEHRYVVLT LLPKAKAAEV
LSHLSPEEQA EYLKTLPPWR LREILEELSL DDLADALQAV RKEDPAYFQR LKDLLDPRTR
AEVEALARYE EDEAGGLMTP EYVAVREGMT VEEVLRFLRR AAPDAETIYY IYVVDEKGRL
KGVLSLRDLI VADPRTRVAE IMNPKVVYVR TDTDQEEVAR LMADYDFTVL PVVDEEGRLV
GIVTVDDVLD VLEAEATEDI HKLGAVDVPD LVYSEAGPVA LWLARVRWLV ILILTGMVTS
SILQGFESVL EAVTALAFYV PVLLGTGGNT GNQSATLIIR ALATRDLDLR DWRRVFLKEM
GVGLLLGLTL SFLLVGKVYW DGHPLLLPVV GVSLVLIVFF ANLVGAMLPF LLRRLGVDPA
LVSNPLVATL SDVTGLLIYL SVARLLLEAV


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