ID U2ZHN4_VIBPR Unreviewed; 467 AA.
AC U2ZHN4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000256|HAMAP-Rule:MF_01128};
GN Name=clcA {ECO:0000256|HAMAP-Rule:MF_01128,
GN ECO:0000313|EMBL:GAD67196.1};
GN ORFNames=VPR01S_06_02150 {ECO:0000313|EMBL:GAD67196.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD67196.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD67196.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD67196.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GAD67196.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BATJ01000006; GAD67196.1; -; Genomic_DNA.
DR RefSeq; WP_021705171.1; NZ_BATJ01000006.1.
DR AlphaFoldDB; U2ZHN4; -.
DR STRING; 1219065.VPR01S_06_02150; -.
DR eggNOG; COG0038; Bacteria.
DR Proteomes; UP000016570; 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 Reference proteome {ECO:0000313|Proteomes:UP000016570};
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 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 73..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..306
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01128"
FT TRANSMEM 326..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..437
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 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 467 AA; 50455 MW; 44FB4EF80D9FA62E CRC64;
MTKREKLKHS LLAHVPKDAI NQFLSKDKTP VSVLLMALLV GILAGVVGTY FEIAVHFVSE
TRTQWLKSEI GSVLPLWLAA FLISATLAFI GYYLVHRFAP EAAGSGIPEI EGAMDGMRPV
RWWRVLPVKF FGGMGALGSG MVLGREGPTV QMGGAIGRMV TDLFRIKNDD TRHSLLASGA
AGGLAAAFNA PLAGIMFVVE EMRPQFRYSL ISIRAVIISA VAANIVFRYI NGQDAVITMP
QYHAPELPAL WLFLLLGALF GVFGVIFNRL VTFSQDMFIR VHKNDRKRYL LTGSLIGGCF
GLMLLYMPEL TGGGIDLIPN ITNGGYGAGL LLLLFLGRII TTMICFSSGA PGGVFAPMLA
LGTLFGYAFG LIASTLLPEL NIQPGMFAIA GMGALFAATV RAPITGILLV IEMTNNYYLI
LPLIITSLGA VIFAQMLGGQ PIYSQLLHRT LKNEKLRQED VPTEAQG
//
