CLCA_CROS8
ID CLCA_CROS8 Reviewed; 467 AA.
AC A7MGR4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN Name=clcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN Synonyms=eriC {ECO:0000255|HAMAP-Rule:MF_01128};
GN OrderedLocusNames=ESA_03185;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78407.1; -; Genomic_DNA.
DR RefSeq; WP_012125720.1; NC_009778.1.
DR AlphaFoldDB; A7MGR4; -.
DR SMR; A7MGR4; -.
DR EnsemblBacteria; ABU78407; ABU78407; ESA_03185.
DR KEGG; esa:ESA_03185; -.
DR PATRIC; fig|290339.8.peg.2816; -.
DR HOGENOM; CLU_015263_7_0_6; -.
DR OMA; PMISGSG; -.
DR OrthoDB; 1560952at2; -.
DR Proteomes; UP000000260; Chromosome.
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..467
FT /note="H(+)/Cl(-) exchange transporter ClcA"
FT /id="PRO_1000065379"
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 TOPO_DOM 99..106
FT /note="Cytoplasmic"
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 TOPO_DOM 140..145
FT /note="Periplasmic"
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 TOPO_DOM 348..352
FT /note="Cytoplasmic"
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..467
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 467 AA; 49730 MW; B094CDB8BBE87255 CRC64;
MKSQTIPTRR VRGFRRAAVI RQLLSRDKTP LTILLLASLT GVLAGLAGVA FEKAVAWVTA
HRIEGLAQVA HIPWLVWLLA FLFSALLAMV GYFLVRRFAP EAGGSGIPEI EGALEELRPV
RWWRVLPVKF FGGMGTLGAG MVLGREGPMV QMGGNIGRMV LDIFHRPDAE ARHTLLATGA
AAGLAAAFNA PLAGILFIIE EMRTQFHYNL ISIKAVFTGV IMSTIVFRIF NGEKSVIEVG
QLTDAPVYTL WLYLLLGIIF GAVGPLFNRL VLGMQDVFAR IHGGNTTRWV LLGGAIGGAC
GLLALWEPAA AGGGFGLIPI AAAGNFTVGM LLFIFIARVV TTVFCFSSGA PGGIFAPMLA
LGTLLGSAFG MACAAWFPQW HLQAGTFAIA GMGALLAASV RAPITGIVLV LEMTDNYQLI
LPMIITCLGA TLLAQFLGGK PLYSTILART LAKQEAERQA QADGRNT
