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Protein

Magnesium transporter MgtE

Gene

TTHA1060

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a highly selective magnesium channel.2 Publications

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Magnesium 1
Metal bindingi95 – 951Magnesium 2
Metal bindingi136 – 1361Magnesium 2; via carbonyl oxygen
Metal bindingi214 – 2141Magnesium 3
Metal bindingi216 – 2161Magnesium 4
Metal bindingi223 – 2231Magnesium 5; via carbonyl oxygen
Metal bindingi226 – 2261Magnesium 5
Metal bindingi247 – 2471Magnesium 1
Metal bindingi255 – 2551Magnesium 3
Metal bindingi258 – 2581Magnesium 3
Metal bindingi259 – 2591Magnesium 4
Metal bindingi418 – 4181Magnesium 4
Metal bindingi428 – 4281Magnesium 6; via carbonyl oxygen
Metal bindingi432 – 4321Magnesium 6

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • magnesium ion transmembrane transporter activity Source: InterPro
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • magnesium ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1319-MONOMER.
TTHE300852:GH8R-1092-MONOMER.
BRENDAi3.6.3.2. 2305.

Protein family/group databases

TCDBi1.A.26.1.2. the mg(2+) transporter-e (mgte) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium transporter MgtE
Gene namesi
Ordered Locus Names:TTHA1060
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 277277CytoplasmicAdd
BLAST
Transmembranei278 – 30528Helical; Name=1Add
BLAST
Intramembranei306 – 32015Add
BLAST
Transmembranei321 – 34424Helical; Name=2Add
BLAST
Topological domaini345 – 3517Cytoplasmic
Transmembranei352 – 38130Helical; Name=3Add
BLAST
Intramembranei382 – 3854
Transmembranei386 – 41429Helical; Name=4Add
BLAST
Intramembranei415 – 42410
Transmembranei425 – 44723Helical; Name=5Add
BLAST
Topological domaini448 – 4503Periplasmic

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591E → A: Still possesses a slight channel activity. 1 Publication
Mutagenesisi226 – 2261D → N: Abolishes the Mg(2+)-dependent suppression of the Mg(2+) influx; when associated with A-250. 1 Publication
Mutagenesisi250 – 2501D → A: Abolishes the Mg(2+)-dependent suppression of the Mg(2+) influx; when associated with N-226. 1 Publication
Mutagenesisi258 – 2581E → Q: Abolishes the Mg(2+)-dependent suppression of the Mg(2+) influx. 1 Publication
Mutagenesisi259 – 2591D → N: Abolishes the Mg(2+)-dependent suppression of the Mg(2+) influx. 1 Publication
Mutagenesisi285 – 2851R → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi318 – 3181F → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi321 – 3211P → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi324 – 3241L → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi329 – 3291N → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi332 – 3321N → A: Does not affect activity. 1 Publication
Mutagenesisi333 – 3331Q → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi359 – 3591E → A: Abolishes Mg(2+)-transport activity. 1 Publication
Mutagenesisi424 – 4241N → A: Does not affect activity. 1 Publication
Mutagenesisi432 – 4321D → A or N: Abolishes Mg(2+)-transport activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Magnesium transporter MgtEPRO_0000363889Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-60248N.
STRINGi300852.TTHA1060.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 93Combined sources
Helixi10 – 156Combined sources
Helixi18 – 2710Combined sources
Helixi30 – 356Combined sources
Helixi36 – 394Combined sources
Helixi42 – 5110Combined sources
Helixi54 – 629Combined sources
Helixi66 – 7510Combined sources
Helixi78 – 8710Combined sources
Helixi90 – 10314Combined sources
Helixi105 – 11410Combined sources
Helixi117 – 12812Combined sources
Helixi134 – 1363Combined sources
Beta strandi142 – 1454Combined sources
Helixi151 – 16111Combined sources
Turni162 – 1643Combined sources
Beta strandi168 – 1747Combined sources
Beta strandi179 – 1857Combined sources
Helixi186 – 1916Combined sources
Turni199 – 2013Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi209 – 2146Combined sources
Helixi215 – 22511Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi237 – 2448Combined sources
Helixi245 – 2517Combined sources
Beta strandi263 – 2653Combined sources
Turni273 – 2753Combined sources
Helixi278 – 29619Combined sources
Helixi298 – 3047Combined sources
Helixi307 – 3126Combined sources
Helixi314 – 3196Combined sources
Helixi320 – 34324Combined sources
Helixi349 – 3513Combined sources
Helixi352 – 38130Combined sources
Helixi384 – 3863Combined sources
Helixi387 – 41428Combined sources
Helixi419 – 4213Combined sources
Helixi423 – 44725Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YVXX-ray3.50A/B/C/D1-450[»]
2YVYX-ray2.30A1-275[»]
2YVZX-ray3.90A/B1-275[»]
2ZY9X-ray2.94A/B1-450[»]
4U9LX-ray2.30A/B271-449[»]
4U9NX-ray2.20A/B271-448[»]
4WIBX-ray3.20A/B271-448[»]
ProteinModelPortaliQ5SMG8.
SMRiQ5SMG8. Positions 7-448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SMG8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 20063CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini202 – 25857CBS 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SLC41A transporter family.Curated
Contains 2 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CJW. Bacteria.
COG2239. LUCA.
HOGENOMiHOG000280152.
KOiK06213.
OMAiLKLSDWW.
OrthoDBiEOG60GRRN.
PhylomeDBiQ5SMG8.

Family and domain databases

Gene3Di1.10.357.20. 1 hit.
InterProiIPR000644. CBS_dom.
IPR006668. Mg_transptr_MgtE_intracell_dom.
IPR006669. MgtE_transporter.
IPR006667. SLC41_membr_dom.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF01769. MgtE. 1 hit.
PF03448. MgtE_N. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 2 hits.
SM00924. MgtE_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00400. mgtE. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SMG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKLAVSLQ EALQEGDTRA LREVLEEIHP QDLLALWDEL KGEHRYVVLT
60 70 80 90 100
LLPKAKAAEV LSHLSPEEQA EYLKTLPPWR LREILEELSL DDLADALQAV
110 120 130 140 150
RKEDPAYFQR LKDLLDPRTR AEVEALARYE EDEAGGLMTP EYVAVREGMT
160 170 180 190 200
VEEVLRFLRR AAPDAETIYY IYVVDEKGRL KGVLSLRDLI VADPRTRVAE
210 220 230 240 250
IMNPKVVYVR TDTDQEEVAR LMADYDFTVL PVVDEEGRLV GIVTVDDVLD
260 270 280 290 300
VLEAEATEDI HKLGAVDVPD LVYSEAGPVA LWLARVRWLV ILILTGMVTS
310 320 330 340 350
SILQGFESVL EAVTALAFYV PVLLGTGGNT GNQSATLIIR ALATRDLDLR
360 370 380 390 400
DWRRVFLKEM GVGLLLGLTL SFLLVGKVYW DGHPLLLPVV GVSLVLIVFF
410 420 430 440 450
ANLVGAMLPF LLRRLGVDPA LVSNPLVATL SDVTGLLIYL SVARLLLEAV
Length:450
Mass (Da):50,078
Last modified:December 21, 2004 - v1
Checksum:i6F5930DCDDB90B05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70883.1.
RefSeqiWP_011228410.1. NC_006461.1.
YP_144326.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70883; BAD70883; BAD70883.
GeneIDi3168925.
KEGGittj:TTHA1060.
PATRICi23957080. VBITheThe93045_1040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70883.1.
RefSeqiWP_011228410.1. NC_006461.1.
YP_144326.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YVXX-ray3.50A/B/C/D1-450[»]
2YVYX-ray2.30A1-275[»]
2YVZX-ray3.90A/B1-275[»]
2ZY9X-ray2.94A/B1-450[»]
4U9LX-ray2.30A/B271-449[»]
4U9NX-ray2.20A/B271-448[»]
4WIBX-ray3.20A/B271-448[»]
ProteinModelPortaliQ5SMG8.
SMRiQ5SMG8. Positions 7-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60248N.
STRINGi300852.TTHA1060.

Protein family/group databases

TCDBi1.A.26.1.2. the mg(2+) transporter-e (mgte) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70883; BAD70883; BAD70883.
GeneIDi3168925.
KEGGittj:TTHA1060.
PATRICi23957080. VBITheThe93045_1040.

Phylogenomic databases

eggNOGiENOG4105CJW. Bacteria.
COG2239. LUCA.
HOGENOMiHOG000280152.
KOiK06213.
OMAiLKLSDWW.
OrthoDBiEOG60GRRN.
PhylomeDBiQ5SMG8.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1319-MONOMER.
TTHE300852:GH8R-1092-MONOMER.
BRENDAi3.6.3.2. 2305.

Miscellaneous databases

EvolutionaryTraceiQ5SMG8.

Family and domain databases

Gene3Di1.10.357.20. 1 hit.
InterProiIPR000644. CBS_dom.
IPR006668. Mg_transptr_MgtE_intracell_dom.
IPR006669. MgtE_transporter.
IPR006667. SLC41_membr_dom.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
PF01769. MgtE. 1 hit.
PF03448. MgtE_N. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 2 hits.
SM00924. MgtE_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00400. mgtE. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Mg(2+)-dependent gating of bacterial MgtE channel underlies Mg(2+) homeostasis."
    Hattori M., Iwase N., Furuya N., Tanaka Y., Tsukazaki T., Ishitani R., Maguire M.E., Ito K., Maturana A., Nureki O.
    EMBO J. 28:3602-3612(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, 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.
  3. "Crystal structure of the MgtE Mg(2+) transporter."
    Hattori M., Tanaka Y., Fukai S., Ishitani R., Nureki O.
    Nature 448:1072-1076(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMGTE_THET8
AccessioniPrimary (citable) accession number: Q5SMG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: December 21, 2004
Last modified: November 11, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.