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Database: UniProt
Entry: A0A061QHX6_9PROT
LinkDB: A0A061QHX6_9PROT
Original site: A0A061QHX6_9PROT 
ID   A0A061QHX6_9PROT        Unreviewed;       491 AA.
AC   A0A061QHX6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Magnesium transporter MgtE {ECO:0000256|RuleBase:RU362011};
GN   Name=mgtE {ECO:0000313|EMBL:GAK33839.1};
GN   ORFNames=AQ1_01731 {ECO:0000313|EMBL:GAK33839.1};
OS   alpha proteobacterium Q-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK33839.1, ECO:0000313|Proteomes:UP000027360};
RN   [1] {ECO:0000313|EMBL:GAK33839.1, ECO:0000313|Proteomes:UP000027360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q-1 {ECO:0000313|EMBL:GAK33839.1,
RC   ECO:0000313|Proteomes:UP000027360};
RX   PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA   Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA   Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT   "Iodide oxidation by a novel multicopper oxidase from the
RT   alphaproteobacterium strain Q-1.";
RL   Appl. Environ. Microbiol. 78:3941-3949(2012).
CC   -!- FUNCTION: Acts as a magnesium transporter.
CC       {ECO:0000256|RuleBase:RU362011}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362011}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362011};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362011}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SLC41A transporter family.
CC       {ECO:0000256|ARBA:ARBA00009749, ECO:0000256|RuleBase:RU362011}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAK33839.1}.
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DR   EMBL; BAYV01000018; GAK33839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061QHX6; -.
DR   STRING; 1492281.AQ1_01731; -.
DR   Proteomes; UP000027360; Unassembled WGS sequence.
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   CDD; cd04606; CBS_pair_Mg_transporter; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 1.25.60.10; MgtE N-terminal domain-like; 1.
DR   Gene3D; 1.10.357.20; SLC41 divalent cation transporters, integral membrane domain; 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   NCBIfam; TIGR00400; mgtE; 1.
DR   PANTHER; PTHR43773; MAGNESIUM TRANSPORTER MGTE; 1.
DR   PANTHER; PTHR43773:SF1; MAGNESIUM TRANSPORTER MGTE; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01769; MgtE; 1.
DR   Pfam; PF03448; MgtE_N; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM00924; MgtE_N; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF161093; MgtE membrane domain-like; 1.
DR   SUPFAM; SSF158791; MgtE N-terminal domain-like; 1.
DR   PROSITE; PS51371; CBS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Cell membrane {ECO:0000256|RuleBase:RU362011};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU362011};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362011};
KW   Metal-binding {ECO:0000256|RuleBase:RU362011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362011};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362011};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362011}.
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362011"
FT   TRANSMEM        354..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362011"
FT   TRANSMEM        402..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362011"
FT   TRANSMEM        430..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362011"
FT   TRANSMEM        463..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362011"
FT   DOMAIN          247..303
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  53397 MW;  B1388609355045A1 CRC64;
     MSAPEDQDDL MTKDPERAQS EHGGEDQSQS KASEIAQDLN YGMDIHLQPD FVRSVIEAVH
     AEDRELARSL VAEQHVADIA DLFEVLPPEE RRTLAVLVAD SLDPIFLSEL EGAAFDDVIR
     VISPQVIADA VQQLDTDDAV YILEDLDADA QHQVLHALTR EDRMALEEGL AFPEDSAGRL
     MQRDLVAVPE FWSVGQTIDY LRAHDDHEQP RDFYELIVID PTYRPIGTVP LSRLLGCQRP
     VRIRDVMTPE PHIVSVSTDQ EEVARQFAKY HLISAGVVNE HGRLVGVITV DDIVGVIEDE
     ASEDILALAG VSEGDVNNSI RDVTRTRFIW LFVNMGTAIL ASMVIGLFEA TLETMVALAV
     LMPIVASMGG NAGTQTMAVA VRALATKELS PANAMRIVNK ELMVALINGA ALAVIVGFVG
     IIWFGDILLA FVLAAAMIIN IVMAGLSGIL IPMMLDRFGI DPAVASSVFV TTITDVVGFF
     AFLGLAALIL I
//
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