MGTE_ENTFA
ID MGTE_ENTFA Reviewed; 453 AA.
AC Q830V1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Magnesium transporter MgtE;
GN Name=mgtE; OrderedLocusNames=EF_2668;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-285.
RX PubMed=17671367; DOI=10.1107/s1744309107032332;
RA Hattori M., Tanaka Y., Fukai S., Ishitani R., Nureki O.;
RT "Crystallization and preliminary X-ray diffraction analysis of the full-
RT length Mg2+ transporter MgtE.";
RL Acta Crystallogr. F 63:682-684(2007).
CC -!- FUNCTION: Acts as a magnesium transporter. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR EMBL; AE016830; AAO82375.1; -; Genomic_DNA.
DR RefSeq; NP_816305.1; NC_004668.1.
DR RefSeq; WP_002362548.1; NZ_KE136528.1.
DR PDB; 2OUX; X-ray; 2.16 A; A/B=2-285.
DR PDBsum; 2OUX; -.
DR AlphaFoldDB; Q830V1; -.
DR SMR; Q830V1; -.
DR STRING; 226185.EF_2668; -.
DR DNASU; 1201525; -.
DR EnsemblBacteria; AAO82375; AAO82375; EF_2668.
DR GeneID; 60894662; -.
DR KEGG; efa:EF2668; -.
DR PATRIC; fig|226185.45.peg.893; -.
DR eggNOG; COG2239; Bacteria.
DR HOGENOM; CLU_037408_2_2_9; -.
DR OMA; TMTVAVR; -.
DR EvolutionaryTrace; Q830V1; -.
DR Proteomes; UP000001415; 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:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..453
FT /note="Magnesium transporter MgtE"
FT /id="PRO_0000363888"
FT TOPO_DOM 1..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 279..306
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT INTRAMEM 307..321
FT /evidence="ECO:0000250"
FT TRANSMEM 322..345
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 346..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 353..383
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT INTRAMEM 384..387
FT /evidence="ECO:0000250"
FT TRANSMEM 388..416
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT INTRAMEM 417..426
FT /evidence="ECO:0000250"
FT TRANSMEM 427..449
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 450..452
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 142..205
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 206..262
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2OUX"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:2OUX"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:2OUX"
SQ SEQUENCE 453 AA; 50320 MW; CDB202115B7BD54F CRC64;
MNEGQEMEEQ FALLLETLKN QQMNEFRELF LALHIYEQGQ FYQSLDEKDR QHLYNYLSPK
ELADMFDVIE EDNENMKDYL AEMRPSYAAD MLAEMYTDNA VDLLNMLDKS QKAKYLSLLS
SEEAGEIKEL LHYEDETAGA IMTTEFVSIV ANQTVRSAMY VLKNQADMAE TIYYVYVVDQ
ENHLVGVISL RDLIVNDDDT LIADILNERV ISVHVGDDQE DVAQTIRDYD FLAVPVTDYD
DHLLGIVTVD DIIDVIDDEA ASDYSGLAGV DVEEVSENPL KAASKRLPWL ITLLFLGMST
ASLISNYESL VSEASILAVF ISLITGTAGN AGTQSLAVAV RRLAMKDEKD SNFGRLILSE
VLTGLVTGAV TGLTIMIVVG VWQHNLPLGF VIGMAMLCAI TVANLAGSLI PMLMDKLGFD
PAVASGPFIT TLSDLTSVLI YFNIASMFMR YFV
