ID Q0ABW0_ALKEH Unreviewed; 288 AA.
AC Q0ABW0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Ion transport protein {ECO:0000313|EMBL:ABI55677.1};
GN OrderedLocusNames=Mlg_0322 {ECO:0000313|EMBL:ABI55677.1};
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI55677.1, ECO:0000313|Proteomes:UP000001962};
RN [1] {ECO:0000313|Proteomes:UP000001962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC {ECO:0000313|Proteomes:UP000001962};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP}
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 143-288 IN COMPLEX WITH CALCIUM.
RX PubMed=24120938; DOI=10.1016/j.jmb.2013.10.010;
RA Shaya D., Findeisen F., Abderemane-Ali F., Arrigoni C., Wong S.,
RA Nurva S.R., Loussouarn G., Minor D.L.;
RT "Structure of a prokaryotic sodium channel pore reveals essential gating
RT elements and an outer ion binding site common to eukaryotic channels.";
RL J. Mol. Biol. 426:467-483(2014).
RN [3] {ECO:0007829|PDB:5HJ8, ECO:0007829|PDB:5HK6}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 143-288.
RX PubMed=26919429; DOI=10.1016/j.cell.2016.02.001;
RA Arrigoni C., Rohaim A., Shaya D., Findeisen F., Stein R.A., Nurva S.R.,
RA Mishra S., Mchaourab H.S., Minor D.L.;
RT "Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel
RT Activation.";
RL Cell 164:922-936(2016).
RN [4] {ECO:0007829|PDB:7PG8, ECO:0007829|PDB:7PGB}
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 143-245.
RX PubMed=35655098; DOI=10.1038/s41594-022-00775-x;
RA Arrigoni C., Lolicato M., Shaya D., Rohaim A., Findeisen F., Fong L.K.,
RA Colleran C.M., Dominik P., Kim S.S., Schuermann J.P., DeGrado W.F.,
RA Grabe M., Kossiakoff A.A., Minor D.L.;
RT "Quaternary structure independent folding of voltage-gated ion channel pore
RT domain subunits.";
RL Nat. Struct. Mol. Biol. 29:537-548(2022).
CC -!- INTERACTION:
CC Q0ABW0; Q0ABW0: Mlg_0322; NbExp=3; IntAct=EBI-15936522, EBI-15936522;
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DR EMBL; CP000453; ABI55677.1; -; Genomic_DNA.
DR RefSeq; WP_011628073.1; NC_008340.1.
DR PDB; 4LTO; X-ray; 3.46 A; A/B/C/D=143-288.
DR PDB; 4LTP; X-ray; 3.80 A; A/B/C/D=143-288.
DR PDB; 4LTQ; X-ray; 5.50 A; A/B/C/D/H/I/J/K=143-288.
DR PDB; 4LTR; X-ray; 5.80 A; A/B/C/D=143-288.
DR PDB; 5HJ8; X-ray; 3.70 A; A/B/C/D=143-288.
DR PDB; 5HK6; X-ray; 5.50 A; A/B/C/D=143-288.
DR PDB; 5HK7; X-ray; 2.95 A; A/B/C/D=143-288.
DR PDB; 5HKD; X-ray; 3.80 A; A/B/C/D=143-288.
DR PDB; 5IWN; X-ray; 3.75 A; A/B/C/D=143-288.
DR PDB; 5IWO; X-ray; 3.33 A; A/B/C/D=143-288.
DR PDB; 7PG8; X-ray; 4.50 A; C/E/H/K/O/Q/T/W=143-245.
DR PDB; 7PGB; X-ray; 3.60 A; C/T/W/Z/c/d/e/h/l/o=143-245.
DR PDB; 7PGH; X-ray; 4.19 A; A/B/C/D/E/F/G/H=143-245.
DR PDBsum; 4LTO; -.
DR PDBsum; 4LTP; -.
DR PDBsum; 4LTQ; -.
DR PDBsum; 4LTR; -.
DR PDBsum; 5HJ8; -.
DR PDBsum; 5HK6; -.
DR PDBsum; 5HK7; -.
DR PDBsum; 5HKD; -.
DR PDBsum; 5IWN; -.
DR PDBsum; 5IWO; -.
DR AlphaFoldDB; Q0ABW0; -.
DR SMR; Q0ABW0; -.
DR DIP; DIP-60398N; -.
DR KEGG; aeh:Mlg_0322; -.
DR eggNOG; ENOG502Z7ZD; Bacteria.
DR HOGENOM; CLU_055047_0_0_6; -.
DR OrthoDB; 5297065at2; -.
DR Proteomes; UP000001962; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005261; F:monoatomic cation channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF62; SODIUM CHANNEL PROTEIN 60E; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP};
KW Calcium {ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP};
KW Reference proteome {ECO:0000313|Proteomes:UP000001962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..244
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:4LTO, ECO:0007829|PDB:4LTP"
SQ SEQUENCE 288 AA; 32978 MW; A3E7B71D2CA35389 CRC64;
MSERQPDLVG HKVQHPEDET LRGRLAWFID RPGTQYFIVG LILVNAITLG LMTSPEVTAY
LQPWLGWVNT FIIAAFVVEI SLRIIADGPR FVRSGWNLFD FSVVAISLVP DSGAFSVLRA
LRILKVLRLF SMVPRLRRIV EALLRAIPGI AWIALLLLVI FYVFAVMGTK LFAQSFPEWF
GTLGASMYTL FQVMTLESWS MGIARPVIEA YPWAWIYFVS FILVSSFTVL NLFIGIIIES
MQSAHWEAED AKRIEQEQRA HDERLEMLQL IRDLSSKVDR LERRSGKR
//
