CLCA_ECOLI
ID CLCA_ECOLI Reviewed; 473 AA.
AC P37019; P77394;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA;
DE AltName: Full=ClC-ec1;
GN Name=clcA; Synonyms=eriC, yadQ; OrderedLocusNames=b0155, JW5012;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY CHARACTERIZATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10539975; DOI=10.1085/jgp.114.5.713;
RA Maduke M., Pheasant D.J., Miller C.;
RT "High-level expression, functional reconstitution, and quaternary structure
RT of a prokaryotic ClC-type chloride channel.";
RL J. Gen. Physiol. 114:713-722(1999).
RN [6]
RP PRELIMINARY CHARACTERIZATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10648805; DOI=10.1016/s0014-5793(99)01740-8;
RA Purdy M.D., Wiener M.C.;
RT "Expression, purification, and initial structural characterization of YadQ,
RT a bacterial homolog of mammalian ClC chloride channel proteins.";
RL FEBS Lett. 466:26-28(2000).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12384697; DOI=10.1038/nature01000;
RA Iyer R., Iverson T.M., Accardi A., Miller C.;
RT "A biological role for prokaryotic ClC chloride channels.";
RL Nature 419:715-718(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-148.
RX PubMed=14985752; DOI=10.1038/nature02314;
RA Accardi A., Miller C.;
RT "Secondary active transport mediated by a prokaryotic homologue of ClC Cl-
RT channels.";
RL Nature 427:803-807(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (6.5 ANGSTROMS).
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11196649; DOI=10.1038/35051631;
RA Mindell J.A., Maduke M., Miller C., Grigorieff N.;
RT "Projection structure of a ClC-type chloride channel at 6.5 A resolution.";
RL Nature 409:219-223(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=11796999; DOI=10.1038/415287a;
RA Dutzler R., Campbell E.B., Cadene M., Chait B.T., MacKinnon R.;
RT "X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular
RT basis of anion selectivity.";
RL Nature 415:287-294(2002).
RN [11] {ECO:0007744|PDB:1OTS, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 17-460 OF MUTANTS ALA-148 AND
RP GLN-148 IN COMPLEX WITH CHLORIDE, AND MUTAGENESIS OF GLU-148.
RX PubMed=12649487; DOI=10.1126/science.1082708;
RA Dutzler R., Campbell E.B., MacKinnon R.;
RT "Gating the selectivity filter in ClC chloride channels.";
RL Science 300:108-112(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), FUNCTION, ION BINDING SITES, AND
RP MUTAGENESIS OF SER-107; GLU-148 AND TYR-445.
RX PubMed=16341087; DOI=10.1038/sj.emboj.7600909;
RA Lobet S., Dutzler R.;
RT "Ion-binding properties of the ClC chloride selectivity filter.";
RL EMBO J. 25:24-33(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-465, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=16905147; DOI=10.1016/j.jmb.2006.07.006;
RA Nguitragool W., Miller C.;
RT "Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions.";
RL J. Mol. Biol. 362:682-690(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), AND MUTAGENESIS OF TYR-445.
RX PubMed=16949616; DOI=10.1016/j.jmb.2006.07.081;
RA Accardi A., Lobet S., Williams C., Miller C., Dutzler R.;
RT "Synergism between halide binding and proton transport in a CLC-type
RT exchanger.";
RL J. Mol. Biol. 362:691-699(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-148/ALA-445, FUNCTION,
RP SUBUNIT, AND MUTAGENESIS OF GLU-148 AND TYR-445.
RX PubMed=18678918; DOI=10.1073/pnas.0804503105;
RA Jayaram H., Accardi A., Wu F., Williams C., Miller C.;
RT "Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+
RT exchanger.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11194-11199(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF MUTANTS HIS-203 AND VAL-203, AND
RP MUTAGENESIS OF GLU-203.
RX PubMed=19139174; DOI=10.1085/jgp.200810112;
RA Lim H.-H., Miller C.;
RT "Intracellular proton-transfer mutants in a CLC Cl-/H+ exchanger.";
RL J. Gen. Physiol. 133:131-138(2009).
CC -!- FUNCTION: Proton-coupled chloride transporter. Functions as antiport
CC system and exchanges two chloride ions for 1 proton. Probably acts as
CC an electrical shunt for an outwardly-directed proton pump that is
CC linked to amino acid decarboxylation, as part of the extreme acid
CC resistance (XAR) response. {ECO:0000269|PubMed:12384697,
CC ECO:0000269|PubMed:14985752, ECO:0000269|PubMed:16341087,
CC ECO:0000269|PubMed:16905147, ECO:0000269|PubMed:18678918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in);
CC Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01128,
CC ECO:0000269|PubMed:14985752, ECO:0000269|PubMed:16905147};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18678918}.
CC -!- INTERACTION:
CC P37019; P37019: clcA; NbExp=7; IntAct=EBI-15719361, EBI-15719361;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: By acid-shock conditions.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcA
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a voltage-gated ClC-type chloride
CC channel. {ECO:0000305}.
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DR EMBL; U70214; AAB08585.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73266.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96732.2; -; Genomic_DNA.
DR PIR; C64739; C64739.
DR RefSeq; NP_414697.1; NC_000913.3.
DR RefSeq; WP_000845394.1; NZ_STEB01000032.1.
DR PDB; 1KPK; X-ray; 3.50 A; A/B/C/D/E/F=1-473.
DR PDB; 1OTS; X-ray; 2.51 A; A/B=1-465.
DR PDB; 1OTT; X-ray; 3.00 A; A/B=1-465.
DR PDB; 1OTU; X-ray; 3.30 A; A/B=1-465.
DR PDB; 2EXW; X-ray; 3.20 A; A/B=1-473.
DR PDB; 2EXY; X-ray; 3.10 A; A/B=1-473.
DR PDB; 2EZ0; X-ray; 3.54 A; A/B=1-473.
DR PDB; 2FEC; X-ray; 3.97 A; A/B=1-465.
DR PDB; 2FED; X-ray; 3.32 A; A/B=1-465.
DR PDB; 2FEE; X-ray; 3.20 A; A/B=1-465.
DR PDB; 2H2P; X-ray; 3.10 A; A/B=1-465.
DR PDB; 2H2S; X-ray; 3.10 A; A/B=1-465.
DR PDB; 2HLF; X-ray; 3.30 A; A/B=17-460.
DR PDB; 2HT2; X-ray; 3.32 A; A/B=1-473.
DR PDB; 2HT3; X-ray; 3.30 A; A/B=1-473.
DR PDB; 2HT4; X-ray; 3.20 A; A/B=1-473.
DR PDB; 2HTK; X-ray; 3.41 A; A/B=1-473.
DR PDB; 2HTL; X-ray; 3.40 A; A/B=1-473.
DR PDB; 2R9H; X-ray; 3.10 A; A/B=17-460.
DR PDB; 3DET; X-ray; 2.80 A; A/B=1-473.
DR PDB; 3EJY; X-ray; 3.20 A; A/B=1-473.
DR PDB; 3EJZ; X-ray; 2.90 A; A/B=1-473.
DR PDB; 3NMO; X-ray; 3.10 A; A=1-465.
DR PDB; 4ENE; X-ray; 2.40 A; A/B=17-460.
DR PDB; 4KJP; X-ray; 3.20 A; A/B=17-460.
DR PDB; 4KJQ; X-ray; 2.88 A; A/B=17-460.
DR PDB; 4KJW; X-ray; 3.03 A; A/B=17-460.
DR PDB; 4KK5; X-ray; 3.17 A; A/B=17-460.
DR PDB; 4KK6; X-ray; 3.18 A; A/B=17-460.
DR PDB; 4KK8; X-ray; 2.86 A; A/B=17-460.
DR PDB; 4KK9; X-ray; 3.00 A; A/B=17-460.
DR PDB; 4KKA; X-ray; 3.00 A; A/B=17-460.
DR PDB; 4KKB; X-ray; 3.02 A; A/B=17-460.
DR PDB; 4KKC; X-ray; 3.18 A; A/B=17-460.
DR PDB; 4KKL; X-ray; 2.85 A; A/B=17-460.
DR PDB; 4LOU; X-ray; 2.98 A; A/B=17-460.
DR PDB; 4MQX; X-ray; 3.52 A; A/B=1-465.
DR PDB; 5HD8; X-ray; 3.15 A; A/B=17-465.
DR PDB; 6AD7; X-ray; 2.95 A; A/B=1-473.
DR PDB; 6AD8; X-ray; 3.30 A; A/B=1-473.
DR PDB; 6ADA; X-ray; 3.15 A; A/B=1-473.
DR PDB; 6ADB; X-ray; 2.69 A; A/B=1-473.
DR PDB; 6ADC; X-ray; 3.06 A; A/B=17-458.
DR PDB; 6K5D; X-ray; 3.20 A; A/B=1-473.
DR PDB; 6K5F; X-ray; 3.20 A; A/B=1-473.
DR PDB; 6LSC; X-ray; 3.21 A; A=1-465.
DR PDB; 6V2J; X-ray; 2.62 A; A=1-468.
DR PDB; 7CVS; X-ray; 3.01 A; A/B=1-473.
DR PDB; 7CVT; X-ray; 2.90 A; A/B=1-473.
DR PDBsum; 1KPK; -.
DR PDBsum; 1OTS; -.
DR PDBsum; 1OTT; -.
DR PDBsum; 1OTU; -.
DR PDBsum; 2EXW; -.
DR PDBsum; 2EXY; -.
DR PDBsum; 2EZ0; -.
DR PDBsum; 2FEC; -.
DR PDBsum; 2FED; -.
DR PDBsum; 2FEE; -.
DR PDBsum; 2H2P; -.
DR PDBsum; 2H2S; -.
DR PDBsum; 2HLF; -.
DR PDBsum; 2HT2; -.
DR PDBsum; 2HT3; -.
DR PDBsum; 2HT4; -.
DR PDBsum; 2HTK; -.
DR PDBsum; 2HTL; -.
DR PDBsum; 2R9H; -.
DR PDBsum; 3DET; -.
DR PDBsum; 3EJY; -.
DR PDBsum; 3EJZ; -.
DR PDBsum; 3NMO; -.
DR PDBsum; 4ENE; -.
DR PDBsum; 4KJP; -.
DR PDBsum; 4KJQ; -.
DR PDBsum; 4KJW; -.
DR PDBsum; 4KK5; -.
DR PDBsum; 4KK6; -.
DR PDBsum; 4KK8; -.
DR PDBsum; 4KK9; -.
DR PDBsum; 4KKA; -.
DR PDBsum; 4KKB; -.
DR PDBsum; 4KKC; -.
DR PDBsum; 4KKL; -.
DR PDBsum; 4LOU; -.
DR PDBsum; 4MQX; -.
DR PDBsum; 5HD8; -.
DR PDBsum; 6AD7; -.
DR PDBsum; 6AD8; -.
DR PDBsum; 6ADA; -.
DR PDBsum; 6ADB; -.
DR PDBsum; 6ADC; -.
DR PDBsum; 6K5D; -.
DR PDBsum; 6K5F; -.
DR PDBsum; 6LSC; -.
DR PDBsum; 6V2J; -.
DR PDBsum; 7CVS; -.
DR PDBsum; 7CVT; -.
DR AlphaFoldDB; P37019; -.
DR PCDDB; P37019; -.
DR SMR; P37019; -.
DR BioGRID; 4259368; 6.
DR DIP; DIP-9523N; -.
DR STRING; 511145.b0155; -.
DR TCDB; 2.A.49.5.1; the chloride carrier/channel (clc) family.
DR jPOST; P37019; -.
DR PaxDb; P37019; -.
DR PRIDE; P37019; -.
DR ABCD; P37019; 1 sequenced antibody.
DR EnsemblBacteria; AAC73266; AAC73266; b0155.
DR EnsemblBacteria; BAB96732; BAB96732; BAB96732.
DR GeneID; 66671556; -.
DR GeneID; 946715; -.
DR KEGG; ecj:JW5012; -.
DR KEGG; eco:b0155; -.
DR PATRIC; fig|1411691.4.peg.2125; -.
DR EchoBASE; EB2235; -.
DR eggNOG; COG0038; Bacteria.
DR HOGENOM; CLU_015263_7_0_6; -.
DR InParanoid; P37019; -.
DR OMA; FAVCVMT; -.
DR PhylomeDB; P37019; -.
DR BioCyc; EcoCyc:YADQ-MON; -.
DR BioCyc; MetaCyc:YADQ-MON; -.
DR EvolutionaryTrace; P37019; -.
DR PRO; PR:P37019; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0062158; F:chloride:proton antiporter activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015299; F:solute:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IBA:GO_Central.
DR GO; GO:1990451; P:cellular stress response to acidic pH; IDA:EcoCyc.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:EcoCyc.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:EcoCyc.
DR HAMAP; MF_01128; CLC_ClcA; 1.
DR InterPro; IPR023861; Cl-channel_ClcA.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; SSF81340; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell inner membrane; Cell membrane; Chloride;
KW Ion transport; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="H(+)/Cl(-) exchange transporter ClcA"
FT /id="PRO_0000094473"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT TRANSMEM 33..69
FT /note="Helical"
FT TOPO_DOM 70..76
FT /note="Periplasmic"
FT TRANSMEM 77..100
FT /note="Helical"
FT INTRAMEM 109..116
FT /note="Helical"
FT TOPO_DOM 117..123
FT /note="Cytoplasmic"
FT TRANSMEM 124..141
FT /note="Helical"
FT TRANSMEM 148..166
FT /note="Helical"
FT TOPO_DOM 167..176
FT /note="Cytoplasmic"
FT INTRAMEM 177..189
FT /note="Helical"
FT INTRAMEM 193..201
FT /note="Helical"
FT TOPO_DOM 202..214
FT /note="Cytoplasmic"
FT TRANSMEM 215..232
FT /note="Helical"
FT TOPO_DOM 233..252
FT /note="Periplasmic"
FT TRANSMEM 253..281
FT /note="Helical"
FT TOPO_DOM 282..287
FT /note="Cytoplasmic"
FT TRANSMEM 288..309
FT /note="Helical"
FT TOPO_DOM 310..329
FT /note="Periplasmic"
FT TRANSMEM 330..349
FT /note="Helical"
FT TRANSMEM 355..376
FT /note="Helical"
FT TOPO_DOM 377..386
FT /note="Periplasmic"
FT INTRAMEM 387..401
FT /note="Helical"
FT INTRAMEM 402..404
FT /note="Note=Loop between two helices"
FT INTRAMEM 405..416
FT /note="Helical"
FT INTRAMEM 417..421
FT /note="Note=Loop between two helices"
FT TRANSMEM 422..438
FT /note="Helical"
FT TOPO_DOM 439..473
FT /note="Cytoplasmic"
FT MOTIF 106..110
FT /note="Selectivity filter part_1"
FT MOTIF 146..150
FT /note="Selectivity filter part_2"
FT MOTIF 355..359
FT /note="Selectivity filter part_3"
FT BINDING 107
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12649487,
FT ECO:0000305|PubMed:16341087, ECO:0000305|PubMed:18678918,
FT ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU"
FT BINDING 356
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12649487,
FT ECO:0007744|PDB:1OTS, ECO:0007744|PDB:4ENE,
FT ECO:0007744|PDB:6LSC"
FT BINDING 357
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12649487,
FT ECO:0007744|PDB:1OTT"
FT BINDING 445
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12649487,
FT ECO:0007744|PDB:1OTS, ECO:0007744|PDB:1OTT,
FT ECO:0007744|PDB:1OTU, ECO:0007744|PDB:4ENE,
FT ECO:0007744|PDB:6LSC"
FT SITE 148
FT /note="Mediates proton transfer from the outer aqueous
FT phase to the interior of the protein; involved in linking
FT H(+) and Cl(-) transport"
FT SITE 203
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT MUTAGEN 107
FT /note="S->A: Uncouples chloride transport from proton
FT transport."
FT /evidence="ECO:0000269|PubMed:16341087"
FT MUTAGEN 148
FT /note="E->A,Q: Abolishes proton transport, but permits the
FT transit of chloride ions. Abolishes gating, permitting
FT continuous rapid transit of chloride ions; when associated
FT with A-445."
FT /evidence="ECO:0000269|PubMed:12649487,
FT ECO:0000269|PubMed:14985752, ECO:0000269|PubMed:16341087,
FT ECO:0000269|PubMed:18678918"
FT MUTAGEN 203
FT /note="E->A,G,Q,S,T: Abolishes proton transport, and
FT reduces chloride transport."
FT /evidence="ECO:0000269|PubMed:19139174"
FT MUTAGEN 203
FT /note="E->C,I,L,V: Abolishes proton and chloride
FT transport."
FT /evidence="ECO:0000269|PubMed:19139174"
FT MUTAGEN 203
FT /note="E->D,H: No effect on proton and chloride transport."
FT /evidence="ECO:0000269|PubMed:19139174"
FT MUTAGEN 203
FT /note="E->K,R: Decreased proton and chloride transport."
FT /evidence="ECO:0000269|PubMed:19139174"
FT MUTAGEN 445
FT /note="Y->A: Abolishes gating, permitting continuous rapid
FT transit of chloride ions; when associated with A-148."
FT /evidence="ECO:0000269|PubMed:16341087,
FT ECO:0000269|PubMed:16949616, ECO:0000269|PubMed:18678918"
FT MUTAGEN 445
FT /note="Y->F,W: No effect."
FT /evidence="ECO:0000269|PubMed:16341087,
FT ECO:0000269|PubMed:16949616, ECO:0000269|PubMed:18678918"
FT MUTAGEN 445
FT /note="Y->L: Alters stoichiometry of proton/chloride
FT exchange."
FT /evidence="ECO:0000269|PubMed:16341087,
FT ECO:0000269|PubMed:16949616, ECO:0000269|PubMed:18678918"
FT CONFLICT 32
FT /note="P -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4ENE"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2HTK"
FT HELIX 33..70
FT /evidence="ECO:0007829|PDB:4ENE"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4ENE"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1KPK"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 215..231
FT /evidence="ECO:0007829|PDB:4ENE"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 252..284
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4ENE"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:6V2J"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 330..348
FT /evidence="ECO:0007829|PDB:4ENE"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4ENE"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 357..378
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:4ENE"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:4ENE"
SQ SEQUENCE 473 AA; 50349 MW; 0B1BC39B417E9690 CRC64;
MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL
QNQRMGALVH TADNYPLLLT VAFLCSAVLA MFGYFLVRKY APEAGGSGIP EIEGALEDQR
PVRWWRVLPV KFFGGLGTLG GGMVLGREGP TVQIGGNIGR MVLDIFRLKG DEARHTLLAT
GAAAGLAAAF NAPLAGILFI IEEMRPQFRY TLISIKAVFI GVIMSTIMYR IFNHEVALID
VGKLSDAPLN TLWLYLILGI IFGIFGPIFN KWVLGMQDLL HRVHGGNITK WVLMGGAIGG
LCGLLGFVAP ATSGGGFNLI PIATAGNFSM GMLVFIFVAR VITTLLCFSS GAPGGIFAPM
LALGTVLGTA FGMVAVELFP QYHLEAGTFA IAGMGALLAA SIRAPLTGII LVLEMTDNYQ
LILPMIITGL GATLLAQFTG GKPLYSAILA RTLAKQEAEQ LARSKAASAS ENT
