CORA_THEMA
ID CORA_THEMA Reviewed; 351 AA.
AC Q9WZ31;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Cobalt/magnesium transport protein CorA {ECO:0000305};
GN Name=corA; OrderedLocusNames=TM_0561;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312; MET-313 AND
RP ASN-314.
RX PubMed=18276588; DOI=10.1074/jbc.m707889200;
RA Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.;
RT "Probing structure-function relationships and gating mechanisms in the CorA
RT Mg2+ transport system.";
RL J. Biol. Chem. 283:11721-11733(2008).
RN [3]
RP FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=21454699; DOI=10.1074/jbc.m111.222166;
RA Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P., Eshaghi S.;
RT "Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate
RT Mg2+ homeostasis present a new class of CorA proteins.";
RL J. Biol. Chem. 286:16525-16532(2011).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF ILE-310;
RP TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
RX PubMed=22722933; DOI=10.1074/jbc.m112.371484;
RA Palombo I., Daley D.O., Rapp M.;
RT "The periplasmic loop provides stability to the open state of the CorA
RT magnesium channel.";
RL J. Biol. Chem. 287:27547-27555(2012).
RN [5]
RP FUNCTION, MUTAGENESIS OF ASN-288, AND SUBCELLULAR LOCATION.
RX PubMed=23091000; DOI=10.1073/pnas.1210076109;
RA Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J.,
RA Cornvik T., Phua T., Eshaghi S.;
RT "Structural insights into the mechanisms of Mg2+ uptake, transport, and
RT gating by CorA.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF TYR-311;
RP GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
RX PubMed=23781956; DOI=10.1021/bi4007397;
RA Palombo I., Daley D.O., Rapp M.;
RT "Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of
RT magnesium transport proteins?";
RL Biochemistry 52:4842-4847(2013).
RN [7] {ECO:0007744|PDB:2HN2}
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, MOTIF, DOMAIN, AND MUTAGENESIS OF ASP-253.
RX PubMed=16902408; DOI=10.1038/sj.emboj.7601269;
RA Payandeh J., Pai E.F.;
RT "A structural basis for Mg2+ homeostasis and the CorA translocation
RT cycle.";
RL EMBO J. 25:3762-3773(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT,
RP TOPOLOGY, DOMAIN, AND MOTIF.
RX PubMed=16598263; DOI=10.1038/nature04642;
RA Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A.,
RA Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.;
RT "Crystal structure of the CorA Mg2+ transporter.";
RL Nature 440:833-837(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT,
RP TOPOLOGY, DOMAIN, AND MOTIF.
RX PubMed=16857941; DOI=10.1126/science.1127121;
RA Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., Nordlund P.;
RT "Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom
RT resolution.";
RL Science 313:354-357(2006).
RN [10] {ECO:0007744|PDB:4EEB, ECO:0007744|PDB:4EED}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN
RP COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND DOMAIN.
RX PubMed=23112165; DOI=10.1073/pnas.1209018109;
RA Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.;
RT "Structural asymmetry in the magnesium channel CorA points to sequential
RT allosteric regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012).
RN [11] {ECO:0007744|PDB:4I0U}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ASP-89; ASN-288; THR-295;
RP THR-299 AND THR-305.
RX PubMed=23425532; DOI=10.1042/bj20121745;
RA Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H.,
RA Eshaghi S.;
RT "Exploring the structure and function of Thermotoga maritima CorA reveals
RT the mechanism of gating and ion selectivity in Co2+/Mg2+ transport.";
RL Biochem. J. 451:365-374(2013).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN
RP COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=26871634; DOI=10.1016/j.cell.2015.12.055;
RA Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P.,
RA Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.;
RT "Cryo-EM Structures of the magnesium channel CorA reveal symmetry break
RT upon gating.";
RL Cell 164:747-756(2016).
CC -!- FUNCTION: Mediates influx of magnesium ions (PubMed:18276588,
CC PubMed:22722933, PubMed:23781956, PubMed:23112165). Mediates Co(2+)
CC uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532). Has high
CC selectivity for Co(2+) (PubMed:21454699, PubMed:23425532). Alternates
CC between open and closed states. Activated by low cytoplasmic Mg(2+)
CC levels. Inactive when cytoplasmic Mg(2+) levels are high
CC (PubMed:23112165, PubMed:23425532, PubMed:26871634).
CC {ECO:0000269|PubMed:18276588, ECO:0000269|PubMed:21454699,
CC ECO:0000269|PubMed:22722933, ECO:0000269|PubMed:23091000,
CC ECO:0000269|PubMed:23112165, ECO:0000269|PubMed:23425532,
CC ECO:0000269|PubMed:23781956, ECO:0000305|PubMed:26871634}.
CC -!- ACTIVITY REGULATION: Inhibited by cobalt hexaammine.
CC {ECO:0000269|PubMed:18276588}.
CC -!- SUBUNIT: Homopentamer (PubMed:22722933, PubMed:23781956,
CC PubMed:16902408, PubMed:16598263, PubMed:16857941, PubMed:23112165,
CC PubMed:23425532, PubMed:26871634). In the absence of Mg(2+),
CC interactions between subunits are weakened, and dimers, trimers and
CC tetramers can be observed in vitro (PubMed:22722933, PubMed:26871634).
CC {ECO:0000269|PubMed:16598263, ECO:0000269|PubMed:16857941,
CC ECO:0000269|PubMed:16902408, ECO:0000269|PubMed:22722933,
CC ECO:0000269|PubMed:23112165, ECO:0000269|PubMed:23425532,
CC ECO:0000269|PubMed:23781956, ECO:0000269|PubMed:26871634}.
CC -!- INTERACTION:
CC Q9WZ31; Q9WZ31: corA; NbExp=19; IntAct=EBI-15578365, EBI-15578365;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:23112165,
CC ECO:0000305|PubMed:16598263, ECO:0000305|PubMed:16857941,
CC ECO:0000305|PubMed:16902408, ECO:0000305|PubMed:18276588,
CC ECO:0000305|PubMed:21454699, ECO:0000305|PubMed:22722933,
CC ECO:0000305|PubMed:23091000, ECO:0000305|PubMed:23425532,
CC ECO:0000305|PubMed:23781956, ECO:0000305|PubMed:26871634}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16598263,
CC ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
CC ECO:0000269|PubMed:23112165, ECO:0000269|PubMed:23425532,
CC ECO:0000269|PubMed:26871634, ECO:0000305|PubMed:23091000}.
CC -!- DOMAIN: The central ion permeation pathway is formed by the first
CC transmembrane domain from each of the five subunits. Mg(2+) binding
CC strengthens interactions between subunits and leads to the formation of
CC a symmetrical homopentamer surrounding a closed ion permeation pathway
CC (PubMed:23091000, PubMed:16902408, PubMed:16598263, PubMed:16857941,
CC PubMed:23112165, PubMed:23425532, PubMed:26871634). Co(2+) binding also
CC induces a conformation change (PubMed:21454699). Low Mg(2+)
CC concentrations trigger both a conformation change within each subunit
CC and a loosening of the interactions between subunits. This results in
CC an open ion conduction pathway. In addition, this results in a less
CC symmetrical shape of the whole complex (PubMed:23112165,
CC PubMed:26871634). {ECO:0000269|PubMed:16598263,
CC ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
CC ECO:0000269|PubMed:21454699, ECO:0000269|PubMed:23112165,
CC ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:26871634,
CC ECO:0000305|PubMed:23091000}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35646.1; -; Genomic_DNA.
DR PIR; H72360; H72360.
DR RefSeq; NP_228371.1; NC_000853.1.
DR RefSeq; WP_004081315.1; NZ_CP011107.1.
DR PDB; 2BBH; X-ray; 1.85 A; A=1-266.
DR PDB; 2BBJ; X-ray; 3.90 A; A/B/D/E/F=1-351.
DR PDB; 2HN2; X-ray; 3.70 A; A/B/C/D/E=1-351.
DR PDB; 2IUB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-351.
DR PDB; 3JCF; X-ray; 3.80 A; A/B/C/D/E=1-351.
DR PDB; 3JCG; X-ray; 7.06 A; A/B/C/D/E=1-351.
DR PDB; 3JCH; X-ray; 7.06 A; A/B/C/D/E=1-351.
DR PDB; 4EEB; X-ray; 3.80 A; A/B/C/D/E=26-351.
DR PDB; 4EED; X-ray; 3.92 A; A/B/C/D/E=26-351.
DR PDB; 4I0U; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-351.
DR PDB; 5JRW; X-ray; 3.30 A; A/B/C/D/E=2-351.
DR PDB; 5JTG; X-ray; 3.05 A; A/B/C/D/E=2-351.
DR PDBsum; 2BBH; -.
DR PDBsum; 2BBJ; -.
DR PDBsum; 2HN2; -.
DR PDBsum; 2IUB; -.
DR PDBsum; 3JCF; -.
DR PDBsum; 3JCG; -.
DR PDBsum; 3JCH; -.
DR PDBsum; 4EEB; -.
DR PDBsum; 4EED; -.
DR PDBsum; 4I0U; -.
DR PDBsum; 5JRW; -.
DR PDBsum; 5JTG; -.
DR AlphaFoldDB; Q9WZ31; -.
DR SASBDB; Q9WZ31; -.
DR SMR; Q9WZ31; -.
DR DIP; DIP-59006N; -.
DR STRING; 243274.THEMA_01870; -.
DR TCDB; 1.A.35.3.2; the cora metal ion transporter (mit) family.
DR EnsemblBacteria; AAD35646; AAD35646; TM_0561.
DR KEGG; tma:TM0561; -.
DR eggNOG; COG0598; Bacteria.
DR InParanoid; Q9WZ31; -.
DR OMA; IQKYFRD; -.
DR OrthoDB; 822653at2; -.
DR BRENDA; 7.2.2.14; 6331.
DR EvolutionaryTrace; Q9WZ31; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0006824; P:cobalt ion transport; IMP:UniProtKB.
DR GO; GO:1903830; P:magnesium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR045861; CorA_cytoplasmic_dom.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR004488; Mg/Co-transport_prot_CorA.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR Pfam; PF01544; CorA; 1.
DR SUPFAM; SSF143865; SSF143865; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
DR TIGRFAMs; TIGR00383; corA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cobalt; Coiled coil;
KW Ion transport; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..351
FT /note="Cobalt/magnesium transport protein CorA"
FT /id="PRO_0000239049"
FT TOPO_DOM 1..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16598263,
FT ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
FT ECO:0000269|PubMed:23112165, ECO:0000269|PubMed:23425532,
FT ECO:0000269|PubMed:26871634"
FT TOPO_DOM 314..324
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16598263,
FT ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
FT ECO:0000269|PubMed:23112165, ECO:0000269|PubMed:23425532,
FT ECO:0000269|PubMed:26871634"
FT TOPO_DOM 346..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT COILED 178..225
FT /evidence="ECO:0000255"
FT MOTIF 312..314
FT /note="Probable selectivity filter"
FT /evidence="ECO:0000305|PubMed:16598263,
FT ECO:0000305|PubMed:16857941, ECO:0000305|PubMed:16902408,
FT ECO:0000305|PubMed:23781956"
FT SITE 288
FT /note="Essential for ion permeation"
FT /evidence="ECO:0000269|PubMed:23091000"
FT SITE 294
FT /note="Important for closing the ion permeation pathway in
FT the closed state"
FT /evidence="ECO:0000269|PubMed:16598263,
FT ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
FT ECO:0000269|PubMed:18276588"
FT SITE 295
FT /note="Threonine that confers selectivity for Co(2+)
FT transport"
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 89
FT /note="D->F,K: Decreases ion transport."
FT /evidence="ECO:0000269|PubMed:18276588,
FT ECO:0000269|PubMed:23425532"
FT MUTAGEN 253
FT /note="D->K: Increases protein stability. Decreases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:16902408,
FT ECO:0000269|PubMed:18276588"
FT MUTAGEN 280
FT /note="L->A: Decreases ion transport."
FT /evidence="ECO:0000269|PubMed:18276588"
FT MUTAGEN 288
FT /note="N->L: Abolishes Co(2+) uptake."
FT /evidence="ECO:0000269|PubMed:23091000,
FT ECO:0000269|PubMed:23425532"
FT MUTAGEN 291
FT /note="M->A: No effect on ion transport."
FT /evidence="ECO:0000269|PubMed:18276588"
FT MUTAGEN 294
FT /note="L->A,V: Increases ion transport by suppression of an
FT obstruction in the transmembrane ion permeation pathway."
FT /evidence="ECO:0000269|PubMed:18276588"
FT MUTAGEN 295
FT /note="T->L: Strongly reduces Co(2+) uptake. Abolishes
FT Co(2+) uptake; when associated with L-299."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 295
FT /note="T->M: Strongly reduces Co(2+) uptake."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 295
FT /note="T->S: No significant decrease of Co(2+) uptake, but
FT abolishes selectivity for Co(2+)."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 299
FT /note="T->L: Reduces Co(2+) uptake. Abolishes Co(2+)
FT uptake; when associated with L-295."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 299
FT /note="T->M: No effect on Co(2+) uptake."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 299
FT /note="T->S: Abolishes Co(2+) uptake."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 303
FT /note="P->A,G,I: Increases ion transport by suppression of
FT a kink in the transmembrane ion permeation pathway."
FT /evidence="ECO:0000269|PubMed:18276588"
FT MUTAGEN 305
FT /note="T->L: Abolishes Co(2+) uptake."
FT /evidence="ECO:0000269|PubMed:23425532"
FT MUTAGEN 310
FT /note="I->A: Increases ion transport."
FT /evidence="ECO:0000269|PubMed:22722933"
FT MUTAGEN 311
FT /note="Y->A: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:22722933,
FT ECO:0000269|PubMed:23781956"
FT MUTAGEN 311
FT /note="Y->F: No effect on pentamerization. No effect on ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 312
FT /note="G->A: No effect on pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:18276588,
FT ECO:0000269|PubMed:22722933"
FT MUTAGEN 312
FT /note="G->F: No effect on pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 313
FT /note="M->A: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:18276588,
FT ECO:0000269|PubMed:22722933"
FT MUTAGEN 313
FT /note="M->C,I,L,V: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 314
FT /note="N->A: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:18276588"
FT MUTAGEN 314
FT /note="N->D,E,T: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 314
FT /note="N->Q: No effect on pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 315
FT /note="F->A: Abolishes pentamerization. Abolishes ion
FT transport."
FT /evidence="ECO:0000269|PubMed:22722933,
FT ECO:0000269|PubMed:23781956"
FT MUTAGEN 315
FT /note="F->W: No effect on pentamerization. Increases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 318
FT /note="M->A: Impairs pentamerization. Decreases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:22722933"
FT MUTAGEN 318
FT /note="M->I,L,V: No effect on pentamerization. Decreases
FT ion transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 321
FT /note="L->A: Impairs pentamerization. Decreases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:22722933"
FT MUTAGEN 321
FT /note="L->I: No effect on pentamerization. Decreases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 321
FT /note="L->V: No effect on pentamerization. No effect on ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 327
FT /note="Y->A: Abolishes pentamerization. Strongly decreases
FT ion transport."
FT /evidence="ECO:0000269|PubMed:22722933,
FT ECO:0000269|PubMed:23781956"
FT MUTAGEN 327
FT /note="Y->F: No effect on pentamerization. Increases ion
FT transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT MUTAGEN 327
FT /note="Y->W: Abolishes pentamerization. Mildly decreases
FT ion transport."
FT /evidence="ECO:0000269|PubMed:23781956"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:4I0U"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2BBH"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:2BBH"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2BBH"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2BBH"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:2BBH"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:4I0U"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2BBH"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 166..197
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 208..242
FT /evidence="ECO:0007829|PDB:2BBH"
FT HELIX 244..272
FT /evidence="ECO:0007829|PDB:4I0U"
FT HELIX 275..310
FT /evidence="ECO:0007829|PDB:4I0U"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4I0U"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:4I0U"
FT HELIX 326..344
FT /evidence="ECO:0007829|PDB:4I0U"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:4I0U"
SQ SEQUENCE 351 AA; 41446 MW; 6A845EC612A4A0BA CRC64;
MEEKRLSAKK GLPPGTLVYT GKYREDFEIE VMNYSIEEFR EFKTTDVESV LPFRDSSTPT
WINITGIHRT DVVQRVGEFF GIHPLVLEDI LNVHQRPKVE FFENYVFIVL KMFTYDKNLH
ELESEQVSLI LTKNCVLMFQ EKIGDVFDPV RERIRYNRGI IRKKRADYLL YSLIDALVDD
YFVLLEKIDD EIDVLEEEVL ERPEKETVQR THQLKRNLVE LRKTIWPLRE VLSSLYRDVP
PLIEKETVPY FRDVYDHTIQ IADTVETFRD IVSGLLDVYL SSVSNKTNEV MKVLTIIATI
FMPLTFIAGI YGMNFEYMPE LRWKWGYPVV LAVMGVIAVI MVVYFKKKKW L
