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CLCA_VIBPA
ID   CLCA_VIBPA              Reviewed;         467 AA.
AC   Q87GZ9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN   Name=clcA {ECO:0000255|HAMAP-Rule:MF_01128}; OrderedLocusNames=VPA1166;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC62509.1; -; Genomic_DNA.
DR   RefSeq; NP_800676.1; NC_004605.1.
DR   RefSeq; WP_005463563.1; NC_004605.1.
DR   AlphaFoldDB; Q87GZ9; -.
DR   SMR; Q87GZ9; -.
DR   STRING; 223926.28809534; -.
DR   EnsemblBacteria; BAC62509; BAC62509; BAC62509.
DR   GeneID; 1191862; -.
DR   KEGG; vpa:VPA1166; -.
DR   PATRIC; fig|223926.6.peg.4091; -.
DR   eggNOG; COG0038; Bacteria.
DR   HOGENOM; CLU_015263_7_0_6; -.
DR   OMA; FAVCVMT; -.
DR   Proteomes; UP000002493; Chromosome 2.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..467
FT                   /note="H(+)/Cl(-) exchange transporter ClcA"
FT                   /id="PRO_0000094481"
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   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   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   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;  50011 MW;  029229D1C278CCD6 CRC64;
     MTKRERIVKS VLAHVPKDAI NQFVSRGSTP FSVLIMAAIV GTLAGFVGTY FELAVHFVSE
     TRTEWLRSEI GSVLPLWLAA VLISALLAFI GYFLVHRFAP EAAGSGIPEI EGAMDNIRPV
     RWWRVLPVKF FGGMGALGSG MVLGREGPTV QMGGAVGRMV TDIFRVKDDD TRHSLLASGA
     AGGLAAAFNA PLAGIMFVVE EMRPQFRYSL ISIRAVIISA IMANIVFRAI NGQDAVITMP
     QYQSPALQTL WLFLLLGALF GVFGVIFNKL ITVAQDSFVA IHKNDRKRYL ITGSILGGVF
     GLLLLYVPQL TGGGIALIPD VTTGNYSISI LVLLFIGRVV TTLLCFGSGA PGGIFAPMLA
     LGTLFGYAFG ASADVLLPTL DIEPGVFAIA GMGALFAATV RAPITGILLV IEMTNNYYLI
     LPLIITCLGA VIVAQLLGGQ PIYSQLLHRT LKNDKLRQQD LPENQAS
 
 
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