ID A0A2N7CY42_9VIBR Unreviewed; 466 AA.
AC A0A2N7CY42;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000256|HAMAP-Rule:MF_01128};
GN Name=clcA {ECO:0000256|HAMAP-Rule:MF_01128};
GN ORFNames=BCU70_10325 {ECO:0000313|EMBL:PMH25437.1};
OS Vibrio sp. 10N.286.49.C2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1880856 {ECO:0000313|EMBL:PMH25437.1, ECO:0000313|Proteomes:UP000235640};
RN [1] {ECO:0000313|Proteomes:UP000235640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10N.286.49.C2 {ECO:0000313|Proteomes:UP000235640};
RA Kauffman K., Hussain F., Yang J., Arevalo P., Brown J., Cutler M.,
RA Kelly L., Polz M.F.;
RT "Nontailed viruses are major unrecognized killers of bacteria in the
RT ocean.";
RL Submitted (JUL-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01128};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01128}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01128};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01128}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01128}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMH25437.1}.
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DR EMBL; MCUT01000116; PMH25437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7CY42; -.
DR OrthoDB; 9767361at2; -.
DR Proteomes; UP000235640; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd01031; EriC; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
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 PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|ARBA:ARBA00022449, ECO:0000256|HAMAP-Rule:MF_01128};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01128};
KW Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|HAMAP-Rule:MF_01128};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01128};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01128};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01128};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01128}; Transport {ECO:0000256|HAMAP-Rule:MF_01128}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 250..268
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 289..307
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT BINDING 105
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT BINDING 354
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT BINDING 355
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT BINDING 443
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01128"
FT SITE 201
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
SQ SEQUENCE 466 AA; 50256 MW; B2AAE9775DAAA3E1 CRC64;
MTKRERFKQS LLARVPKETI NQFLSRDKTP VSVLFLSCIV GILAGLVGTL FELGVHFVTD
TRTEWLKDEI GSVLPLWASA FLISACLAFV GYFLVHKFAP EAAGSGIPEI EGAMDNMRPV
RWWRVLPVKF FGGLGALGSG MVLGREGPTV QMGGNLARMV TDIFRVKDDD SRHTLLASGA
AGGLAAAFNS PLAGIMFVVE EMRPHFRYSL ISIKAVLISA VSATIVFRTI NGQDAVITMP
QYDSPSMQVL WLFLVLGALF GVFGVAFNRL ITLFQDLFAK LHKNDLKRFL ITGSLIGGLF
GLLLLYIPEL TGGGIGLIPN ITNGDFGAGF LFVLFIGRVL TTLICFGSGA PGGIFAPMLA
LGTSFGYAFG LIAKLIFPDL PIEPGVFAIA GMGALFSATV RAPITGILLV IEMTNNYHLI
LPLIITALGA TIVAQMLGGQ PIYCQLLHRT LKNTKLKQED LPSKEN
//