CLCA_SHISS
ID CLCA_SHISS Reviewed; 473 AA.
AC Q3Z5K2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SSON_0167;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86960.1; -; Genomic_DNA.
DR PDB; 4FG6; X-ray; 3.02 A; A/B=1-465.
DR PDBsum; 4FG6; -.
DR AlphaFoldDB; Q3Z5K2; -.
DR SMR; Q3Z5K2; -.
DR DIP; DIP-60056N; -.
DR EnsemblBacteria; AAZ86960; AAZ86960; SSON_0167.
DR KEGG; ssn:SSON_0167; -.
DR HOGENOM; CLU_015263_7_0_6; -.
DR OMA; FAVCVMT; -.
DR Proteomes; UP000002529; 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 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell inner membrane; Cell membrane; Chloride;
KW Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="H(+)/Cl(-) exchange transporter ClcA"
FT /id="PRO_0000301545"
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..473
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"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 33..70
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 75..99
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:4FG6"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4FG6"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 252..284
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 330..349
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 357..378
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 422..437
FT /evidence="ECO:0007829|PDB:4FG6"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:4FG6"
SQ SEQUENCE 473 AA; 50349 MW; 0B1BC39B417E9690 CRC64;
MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL
QNQRMGALVH TADNYPLLLT VAFLCSAVLA MFGYFLVRKY APEAGGSGIP EIEGALEDQR
PVRWWRVLPV KFFGGLGTLG GGMVLGREGP TVQIGGNIGR MVLDIFRLKG DEARHTLLAT
GAAAGLAAAF NAPLAGILFI IEEMRPQFRY TLISIKAVFI GVIMSTIMYR IFNHEVALID
VGKLSDAPLN TLWLYLILGI IFGIFGPIFN KWVLGMQDLL HRVHGGNITK WVLMGGAIGG
LCGLLGFVAP ATSGGGFNLI PIATAGNFSM GMLVFIFVAR VITTLLCFSS GAPGGIFAPM
LALGTVLGTA FGMVAVELFP QYHLEAGTFA IAGMGALLAA SIRAPLTGII LVLEMTDNYQ
LILPMIITGL GATLLAQFTG GKPLYSAILA RTLAKQEAEQ LARSKAASAS ENT
