(data stored in ACNUC7421 zone)

SWISSPROT: CLCA_ECO27

ID   CLCA_ECO27              Reviewed;         473 AA.
AC   B7UIK2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
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=E2348C_0162;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Proton-coupled chloride transporter. Functions as
CC       antiport system and exchanges two chloride ions for 1 proton.
CC       Probably acts as an electrical shunt for an outwardly-directed
CC       proton pump that is linked to amino acid decarboxylation, as part
CC       of the extreme acid resistance (XAR) response. {ECO:0000255|HAMAP-
CC       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.
CC       ClcA subfamily. {ECO:0000255|HAMAP-Rule:MF_01128}.
DR   EMBL; FM180568; CAS07710.1; -; Genomic_DNA.
DR   RefSeq; WP_000845394.1; NC_011601.1.
DR   SMR; B7UIK2; -.
DR   EnsemblBacteria; CAS07710; CAS07710; E2348C_0162.
DR   KEGG; ecg:E2348C_0162; -.
DR   KO; K03281; -.
DR   OMA; TPITAMF; -.
DR   BioCyc; ECOL574521:E2348C_RS00835-MONOMER; -.
DR   Proteomes; UP000008205; 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   Gene3D; 1.10.3080.10; -; 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   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SUPFAM; SSF81340; SSF81340; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIK2.
DR   SWISS-2DPAGE; B7UIK2.
KW   Antiport; Cell inner membrane; Cell membrane; Chloride;
KW   Complete proteome; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    473       H(+)/Cl(-) exchange transporter ClcA.
FT                                /FTId=PRO_1000164069.
FT   TOPO_DOM      1     32       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM     33     69       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM     70     76       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM     77    100       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    109    116       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    117    123       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    124    141       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    148    166       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    167    176       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    177    189       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    193    201       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    202    214       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    215    232       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    233    252       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    253    281       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    282    287       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    288    309       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    310    329       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    330    349       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TRANSMEM    355    376       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    377    386       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    387    401       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    402    404       Note=Loop between two helices.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   INTRAMEM    405    416       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   INTRAMEM    417    421       Note=Loop between two helices.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   TRANSMEM    422    438       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   TOPO_DOM    439    473       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   MOTIF       106    110       Selectivity filter part_1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   MOTIF       146    150       Selectivity filter part_2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   MOTIF       355    359       Selectivity filter part_3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   BINDING     107    107       Chloride. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   BINDING     356    356       Chloride; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   BINDING     357    357       Chloride; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
FT   BINDING     445    445       Chloride. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   SITE        148    148       Mediates proton transfer from the outer
FT                                aqueous phase to the interior of the
FT                                protein; involved in linking H(+) and
FT                                Cl(-) transport. {ECO:0000255|HAMAP-
FT                                Rule:MF_01128}.
FT   SITE        203    203       Mediates proton transfer from the protein
FT                                to the inner aqueous phase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01128}.
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
//

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