CLCA_SALTY
ID CLCA_SALTY Reviewed; 473 AA.
AC Q8ZRP8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA;
GN Name=clcA; Synonyms=eriC; OrderedLocusNames=STM0203;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND FUNCTION.
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).
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:0000255|HAMAP-Rule:MF_01128,
CC ECO:0000269|PubMed:11796999}.
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcA
CC subfamily. {ECO:0000305}.
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DR EMBL; AE006468; AAL19167.1; -; Genomic_DNA.
DR RefSeq; NP_459208.1; NC_003197.2.
DR RefSeq; WP_000845427.1; NC_003197.2.
DR PDB; 1KPL; X-ray; 3.00 A; A/B/C/D=1-473.
DR PDBsum; 1KPL; -.
DR AlphaFoldDB; Q8ZRP8; -.
DR SMR; Q8ZRP8; -.
DR STRING; 99287.STM0203; -.
DR PaxDb; Q8ZRP8; -.
DR ABCD; Q8ZRP8; 1 sequenced antibody.
DR EnsemblBacteria; AAL19167; AAL19167; STM0203.
DR GeneID; 1251721; -.
DR KEGG; stm:STM0203; -.
DR PATRIC; fig|99287.12.peg.216; -.
DR HOGENOM; CLU_015263_7_0_6; -.
DR PhylomeDB; Q8ZRP8; -.
DR BioCyc; SENT99287:STM0203-MON; -.
DR EvolutionaryTrace; Q8ZRP8; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="H(+)/Cl(-) exchange transporter ClcA"
FT /id="PRO_0000094478"
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 190..192
FT /note="Note=Loop between two helices"
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..308
FT /note="Helical"
FT TOPO_DOM 309..329
FT /note="Periplasmic"
FT TRANSMEM 330..349
FT /note="Helical"
FT TOPO_DOM 350..354
FT /note="Cytoplasmic"
FT TRANSMEM 355..378
FT /note="Helical"
FT TOPO_DOM 379..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 BINDING 356
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 357
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 445
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
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 HELIX 13..25
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 32..66
FT /evidence="ECO:0007829|PDB:1KPL"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 75..99
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:1KPL"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 215..233
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 252..284
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1KPL"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1KPL"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:1KPL"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 357..378
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:1KPL"
FT HELIX 444..459
FT /evidence="ECO:0007829|PDB:1KPL"
SQ SEQUENCE 473 AA; 50481 MW; 7134B5A5510A65A1 CRC64;
MKTDTSTFLA QQIVRLRRRD QIRRLMQRDK TPLAILFMAA VVGTLTGLVG VAFEKAVSWV
QNMRIGALVQ VADHAFLLWP LAFILSALLA MVGYFLVRKF APEAGGSGIP EIEGALEELR
PVRWWRVLPV KFIGGMGTLG AGMVLGREGP TVQIGGNLGR MVLDVFRMRS AEARHTLLAT
GAAAGLSAAF NAPLAGILFI IEEMRPQFRY NLISIKAVFT GVIMSSIVFR IFNGEAPIIE
VGKLSDAPVN TLWLYLILGI IFGCVGPVFN SLVLRTQDMF QRFHGGEIKK WVLMGGAIGG
LCGILGLIEP AAAGGGFNLI PIAAAGNFSV GLLLFIFITR VVTTLLCFSS GAPGGIFAPM
LALGTLLGTA FGMAAAVLFP QYHLEAGTFA IAGMGALMAA SVRAPLTGIV LVLEMTDNYQ
LILPMIITCL GATLLAQFLG GKPLYSTILA RTLAKQDAEQ AEKNQNAPAD ENT
