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Database: UniProt
Entry: A0A2N7CY42_9VIBR
LinkDB: A0A2N7CY42_9VIBR
Original site: A0A2N7CY42_9VIBR 
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
//
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