CLCA_VIBCH
ID CLCA_VIBCH Reviewed; 468 AA.
AC Q9KM62;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN Name=clcA {ECO:0000255|HAMAP-Rule:MF_01128}; OrderedLocusNames=VC_A0526;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- 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. {ECO:0000255|HAMAP-Rule:MF_01128}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01128}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01128}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01128}.
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DR EMBL; AE003853; AAF96429.1; -; Genomic_DNA.
DR PIR; C82449; C82449.
DR RefSeq; NP_232917.1; NC_002506.1.
DR RefSeq; WP_000107451.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KM62; -.
DR SMR; Q9KM62; -.
DR STRING; 243277.VC_A0526; -.
DR DNASU; 2612726; -.
DR EnsemblBacteria; AAF96429; AAF96429; VC_A0526.
DR GeneID; 57741929; -.
DR KEGG; vch:VC_A0526; -.
DR PATRIC; fig|243277.26.peg.3151; -.
DR eggNOG; COG0038; Bacteria.
DR HOGENOM; CLU_015263_7_0_6; -.
DR OMA; PMISGSG; -.
DR BioCyc; VCHO:VCA0526-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Chloride; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..468
FT /note="H(+)/Cl(-) exchange transporter ClcA"
FT /id="PRO_0000094480"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 31..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 68..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 107..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 115..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 122..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 165..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 175..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 191..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 200..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 213..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 231..250
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 251..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 280..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 308..327
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 353..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 375..384
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 385..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 400..402
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 403..414
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT INTRAMEM 415..419
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TRANSMEM 420..436
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT TOPO_DOM 437..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT MOTIF 104..108
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT MOTIF 144..148
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT MOTIF 353..357
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT BINDING 105
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT BINDING 354
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT BINDING 355
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT BINDING 443
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT SITE 146
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 /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT SITE 201
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
SQ SEQUENCE 468 AA; 50520 MW; E5BA18CA6BAE6AA8 CRC64;
MSTRETFKIS LLAKMPKDVI NQFLSKDKTP FSVLFLSLLV GILAGLVGTY FEQAVHLVSE
TRTDWLKSEI GSFLPLWLAA FLISAFLAFI GYFLVHRFAP EAAGSGIPEI EGAMDGMRPV
RWWRVLPVKF FGGMGALGSG MVLGREGPTV QMGGAVGRMI SDIFRVKNED TRHSLLAAGA
AGGLAAAFNA PLAGIMFVIE EMRPQFRYTL ISVRAVIISA VAANIVFRVI NGQDAVITMP
QYDAPELSTL GLFLLLGALF GVFGVLFNYL ITLAQDLFVK FHRNDRKRYL LTGSMIGGCF
GLLLLYVPEL TGGGISLIPT ITNGGYGAGI LLLLFVGRIF TTLLCFGSGA PGGIFAPMLA
LGTLFGYAFG LIAKMWFPEL NIEPGMFAIA GMGALFAATV RAPITGILLV IEMTNNYHLI
LPLIITSLGA VIFAQLLGGQ PIYSQLLHRT LKNQKLQQQD LPPQSPNS
