位置:首页 > 蛋白库 > CLCA_VIBC3
CLCA_VIBC3
ID   CLCA_VIBC3              Reviewed;         468 AA.
AC   A5F0D5; C3M669;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=H(+)/Cl(-) exchange transporter ClcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN   Name=clcA {ECO:0000255|HAMAP-Rule:MF_01128};
GN   OrderedLocusNames=VC0395_0459, VC395_A0798;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000626; ABQ19055.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11632.1; -; Genomic_DNA.
DR   RefSeq; WP_000107452.1; NZ_JAACZH010000019.1.
DR   AlphaFoldDB; A5F0D5; -.
DR   SMR; A5F0D5; -.
DR   STRING; 345073.VC395_A0798; -.
DR   EnsemblBacteria; ABQ19055; ABQ19055; VC0395_0459.
DR   KEGG; vco:VC0395_0459; -.
DR   KEGG; vcr:VC395_A0798; -.
DR   PATRIC; fig|345073.21.peg.3530; -.
DR   eggNOG; COG0038; Bacteria.
DR   HOGENOM; CLU_015263_7_0_6; -.
DR   OMA; PMISGSG; -.
DR   Proteomes; UP000000249; Chromosome 1.
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..468
FT                   /note="H(+)/Cl(-) exchange transporter ClcA"
FT                   /id="PRO_1000073047"
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..468
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   468 AA;  50488 MW;  11EB5DCB3BB4C1B2 CRC64;
     MSTRETFKIS LLAKMPKDVI NQFLSKDKTP FSVLFLSLLV GILAGLVGTY FEQAVHLVSE
     TRTDWLKSEI GSFLPLWLAA FLISAFLAFI GYFLVHRFAP EAAGSGIPEI EGAMDGMRPV
     RWWRVLPVKF FGGMGALGSG MVLGREGPTV QMGGAVGRMI SDIFRVKNED TRHSLLAAGA
     AGGLAAAFNA PLAGIMFVIE EMRPQFRYTL ISVRAVIISA VAANIVFRVI NGQDAVITMP
     QYDAPELSTL GLFLLLGALF GVFGVLFNYL ITLAQDLFVK FHRNDRKRYL LTGSMIGGCF
     GLLLLYVPEL TGGGISLIPT ITNGGYGAGI LLLLFVGRIF TTLLCFGSGA PGGIFAPMLA
     LGTLFGYAFG LIAKVWFPEL NIEPGMFAIA GMGALFAATV RAPITGILLV IEMTNNYHLI
     LPLIITSLGA VIFAQLLGGQ PIYSQLLHRT LKNQKLQQQD LPPQSPNS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024