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CLCA_VIBC1
ID   CLCA_VIBC1              Reviewed;         468 AA.
AC   A7N6K9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN   Name=clcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN   OrderedLocusNames=VIBHAR_06233;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000790; ABU74125.1; -; Genomic_DNA.
DR   RefSeq; WP_012129713.1; NC_022270.1.
DR   AlphaFoldDB; A7N6K9; -.
DR   SMR; A7N6K9; -.
DR   EnsemblBacteria; ABU74125; ABU74125; VIBHAR_06233.
DR   KEGG; vha:VIBHAR_06233; -.
DR   PATRIC; fig|338187.25.peg.4105; -.
DR   OMA; FAVCVMT; -.
DR   OrthoDB; 1560952at2; -.
DR   Proteomes; UP000008152; Chromosome II.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..468
FT                   /note="H(+)/Cl(-) exchange transporter ClcA"
FT                   /id="PRO_1000065381"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        33..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        70..76
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        77..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        109..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        117..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        124..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        167..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        177..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        193..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        202..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        215..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        233..252
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        253..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        282..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        288..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        310..329
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        330..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        355..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        377..386
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        387..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        402..404
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        405..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   INTRAMEM        417..421
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TRANSMEM        422..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   TOPO_DOM        439..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   MOTIF           106..110
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   MOTIF           146..150
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   MOTIF           355..359
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   BINDING         107
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   BINDING         356
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   BINDING         357
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   BINDING         445
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
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                   /evidence="ECO:0000255|HAMAP-Rule:MF_01128"
FT   SITE            203
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;  50174 MW;  5A84CAC0D67D85FD CRC64;
     MIKRERIVKS VLAHVPKDAI NQFVSRGSTP TSFSVLFMAA IVGTLAGLVG TYFEIAVHFV
     SETRTEWLKS EIGSVLPLWL AAILISGALA FIGYYLVNRF APEASGSGIP EIEGAMDNIR
     SVRWWRVIPV KFFGGMGALG SGMVLGREGP TVQMGGAVGR MVTDIFRVKD DDTRHSLLAS
     GAAGGLAAAF NAPLAAIMFV VEEMRPQFRY SLISIRAVII SAIMANIVFR AINGQEAVIT
     MPQYQSPELQ SLWLFLLLGS LFGVFGVVFN KLITIAQDSF VALHKNDRKR YLITGTILGG
     VFGLLLLYVP QLTGGGIGLI PDITNGNYSI SILVMLFVGR VITTLLCFGS GAPGGIFAPM
     LALGTLFGYA FGASADMLLP SLTIEPGVFA IAGMGALFAA TVRAPITGIL LVIEMTNNYY
     LILPLIITSL GAVIVAQLLG GQPIYSQLLH RTLKNDKLRQ QDLPENQA
 
 
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