MGTE_THET8
ID MGTE_THET8 Reviewed; 450 AA.
AC Q5SMG8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Magnesium transporter MgtE;
GN OrderedLocusNames=TTHA1060;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-59; ASP-226; ASP-250;
RP GLU-258; ASP-259; ARG-285; PHE-318; PRO-321; LEU-324; ASN-329; ASN-332;
RP GLN-333; GLU-359; ASN-424 AND ASP-432.
RX PubMed=19798051; DOI=10.1038/emboj.2009.288;
RA Hattori M., Iwase N., Furuya N., Tanaka Y., Tsukazaki T., Ishitani R.,
RA Maguire M.E., Ito K., Maturana A., Nureki O.;
RT "Mg(2+)-dependent gating of bacterial MgtE channel underlies Mg(2+)
RT homeostasis.";
RL EMBO J. 28:3602-3612(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17700703; DOI=10.1038/nature06093;
RA Hattori M., Tanaka Y., Fukai S., Ishitani R., Nureki O.;
RT "Crystal structure of the MgtE Mg(2+) transporter.";
RL Nature 448:1072-1076(2007).
CC -!- FUNCTION: Acts as a highly selective magnesium channel.
CC {ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:19798051}.
CC -!- ACTIVITY REGULATION: The channel activity is regulated by the
CC intracellular magnesium concentration. Under high-intracellular
CC magnesium conditions, binding of magnesium to the cytosolic domains
CC stabilizes the closed conformation of the channel. Under low-
CC intracellular magnesium conditions, the channel is in equilibrium
CC between the open and closed states. {ECO:0000269|PubMed:19798051}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17700703}.
CC -!- INTERACTION:
CC Q5SMG8; Q5SMG8: TTHA1060; NbExp=2; IntAct=EBI-15652583, EBI-15652583;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17700703};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17700703}.
CC -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR EMBL; AP008226; BAD70883.1; -; Genomic_DNA.
DR RefSeq; WP_011228410.1; NC_006461.1.
DR RefSeq; YP_144326.1; NC_006461.1.
DR PDB; 2YVX; X-ray; 3.50 A; A/B/C/D=1-450.
DR PDB; 2YVY; X-ray; 2.30 A; A=1-275.
DR PDB; 2YVZ; X-ray; 3.90 A; A/B=1-275.
DR PDB; 2ZY9; X-ray; 2.94 A; A/B=1-450.
DR PDB; 4U9L; X-ray; 2.30 A; A/B=271-449.
DR PDB; 4U9N; X-ray; 2.20 A; A/B=271-448.
DR PDB; 4WIB; X-ray; 3.20 A; A/B=271-448.
DR PDB; 5X9G; X-ray; 3.00 A; A/B/C/D=1-275.
DR PDB; 5X9H; X-ray; 3.60 A; A/B=1-450.
DR PDB; 6LBH; EM; 3.70 A; A/B=271-448.
DR PDBsum; 2YVX; -.
DR PDBsum; 2YVY; -.
DR PDBsum; 2YVZ; -.
DR PDBsum; 2ZY9; -.
DR PDBsum; 4U9L; -.
DR PDBsum; 4U9N; -.
DR PDBsum; 4WIB; -.
DR PDBsum; 5X9G; -.
DR PDBsum; 5X9H; -.
DR PDBsum; 6LBH; -.
DR AlphaFoldDB; Q5SMG8; -.
DR SMR; Q5SMG8; -.
DR DIP; DIP-60248N; -.
DR STRING; 300852.55772442; -.
DR TCDB; 1.A.26.1.2; the mg(2+) transporter-e (mgte) family.
DR EnsemblBacteria; BAD70883; BAD70883; BAD70883.
DR GeneID; 3168925; -.
DR KEGG; ttj:TTHA1060; -.
DR PATRIC; fig|300852.9.peg.1040; -.
DR eggNOG; COG2239; Bacteria.
DR HOGENOM; CLU_037408_2_2_0; -.
DR OMA; TMTVAVR; -.
DR PhylomeDB; Q5SMG8; -.
DR BRENDA; 7.2.2.14; 2305.
DR EvolutionaryTrace; Q5SMG8; -.
DR Proteomes; UP000000532; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0015693; P:magnesium ion transport; NAS:UniProtKB.
DR Gene3D; 1.10.357.20; -; 1.
DR Gene3D; 1.25.60.10; -; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR006668; Mg_transptr_MgtE_intracell_dom.
DR InterPro; IPR038076; MgtE_N_sf.
DR InterPro; IPR006669; MgtE_transporter.
DR InterPro; IPR006667; SLC41_membr_dom.
DR InterPro; IPR036739; SLC41_membr_dom_sf.
DR PANTHER; PTHR43773; PTHR43773; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01769; MgtE; 1.
DR Pfam; PF03448; MgtE_N; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00924; MgtE_N; 1.
DR SUPFAM; SSF161093; SSF161093; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR00400; mgtE; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; CBS domain; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..450
FT /note="Magnesium transporter MgtE"
FT /id="PRO_0000363889"
FT TOPO_DOM 1..277
FT /note="Cytoplasmic"
FT TRANSMEM 278..305
FT /note="Helical; Name=1"
FT INTRAMEM 306..320
FT TRANSMEM 321..344
FT /note="Helical; Name=2"
FT TOPO_DOM 345..351
FT /note="Cytoplasmic"
FT TRANSMEM 352..381
FT /note="Helical; Name=3"
FT INTRAMEM 382..385
FT TRANSMEM 386..414
FT /note="Helical; Name=4"
FT INTRAMEM 415..424
FT TRANSMEM 425..447
FT /note="Helical; Name=5"
FT TOPO_DOM 448..450
FT /note="Periplasmic"
FT DOMAIN 138..200
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 202..258
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="6"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="6"
FT MUTAGEN 59
FT /note="E->A: Still possesses a slight channel activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 226
FT /note="D->N: Abolishes the Mg(2+)-dependent suppression of
FT the Mg(2+) influx; when associated with A-250."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 250
FT /note="D->A: Abolishes the Mg(2+)-dependent suppression of
FT the Mg(2+) influx; when associated with N-226."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 258
FT /note="E->Q: Abolishes the Mg(2+)-dependent suppression of
FT the Mg(2+) influx."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 259
FT /note="D->N: Abolishes the Mg(2+)-dependent suppression of
FT the Mg(2+) influx."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 285
FT /note="R->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 318
FT /note="F->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 321
FT /note="P->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 324
FT /note="L->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 329
FT /note="N->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 332
FT /note="N->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 333
FT /note="Q->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 359
FT /note="E->A: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 424
FT /note="N->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT MUTAGEN 432
FT /note="D->A,N: Abolishes Mg(2+)-transport activity."
FT /evidence="ECO:0000269|PubMed:19798051"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2ZY9"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:2YVY"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:2YVY"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2ZY9"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2YVY"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:2YVY"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2YVX"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 278..296
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 320..343
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 352..381
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 387..414
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4U9N"
FT HELIX 423..447
FT /evidence="ECO:0007829|PDB:4U9N"
SQ 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
