ID A0A0C2LPN8_9CYAN Unreviewed; 466 AA.
AC A0A0C2LPN8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Magnesium transporter MgtE {ECO:0000256|RuleBase:RU362011};
GN ORFNames=SD81_20625 {ECO:0000313|EMBL:KIJ76731.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ76731.1};
RN [1] {ECO:0000313|EMBL:KIJ76731.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ76731.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIJ76731.1}.
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DR EMBL; JXCB01000008; KIJ76731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2LPN8; -.
DR OrthoDB; 9790355at2; -.
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; 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; 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; 2.
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 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 302..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362011"
FT TRANSMEM 325..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362011"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362011"
FT TRANSMEM 403..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362011"
FT TRANSMEM 441..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362011"
FT DOMAIN 153..216
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 217..273
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 466 AA; 51292 MW; CCF05ACDF7A2A1F8 CRC64;
MQTPNGMTST FQDVSRRELR ELVRVQLQML LEAGDLQGAK AILVPVQPAD IAEAIEGLPE
AMHALAFRLL SKQEAIEVYE YLDYSVQERL IEELRSQEVL HIVDKMSPDD RARLFDELPA
KIVNRLLEQL SPNERQATAQ LLGYEAGTAG RIMTPELISL KENFTVAETL ERIRRLANAS
EMIYYLYVTD AARRLTGILS LRELVTSQPE QRIGDVMTRE AVFIYTDTDQ EEVARLIQRY
DFLAVPVVDR EQRLVGIVTV DDVIDILQQE TTEDIYTLGG GVQSGGDNYF QLDLISVARK
RVVWLLVLLV TNTVTGTIIR SQEDILAKVV SLAAFIPLLT GTGGNVGAQS STVVIRGMNT
DEIRALGPLQ VIGREGLAGA LLGGILGTIA TVWAFFLQKN LEVAIAVGIS LVAISVLASV
SGSALPFLFR LLRLDPALMS APFITTAVDV LGVLIYFSLA RVILKV
//
