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CLCB_ECOL6
ID   CLCB_ECOL6              Reviewed;         418 AA.
AC   Q8FHC1;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Voltage-gated ClC-type chloride channel ClcB;
GN   Name=clcB; OrderedLocusNames=c1983;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Probably acts as an electrical shunt for an outwardly-
CC       directed proton pump that is linked to amino acid decarboxylation, as
CC       part of the extreme acid resistance (XAR) response. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcB
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN80443.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FHC1; -.
DR   SMR; Q8FHC1; -.
DR   STRING; 199310.c1983; -.
DR   TCDB; 2.A.49.5.3; the chloride carrier/channel (clc) family.
DR   EnsemblBacteria; AAN80443; AAN80443; c1983.
DR   KEGG; ecc:c1983; -.
DR   eggNOG; COG0038; Bacteria.
DR   HOGENOM; CLU_015263_5_2_6; -.
DR   OMA; GPLTMTF; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0010447; P:response to acidic pH; IEA:InterPro.
DR   HAMAP; MF_01203; CLC_ClcB; 1.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR023790; Cl-channel_volt-gated_ClcB.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SUPFAM; SSF81340; SSF81340; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chloride; Chloride channel;
KW   Ion channel; Ion transport; Membrane; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN           1..418
FT                   /note="Voltage-gated ClC-type chloride channel ClcB"
FT                   /id="PRO_0000094486"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..53
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..177
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..257
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..290
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..315
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..379
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..418
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  44139 MW;  8DBF5BBDA7AC21A0 CRC64;
     MFRRLLIATI VGILAAFAVA GFRHAMLLLE WLFLNNDSGS LVNAATNLSP WRRLLTPALG
     GLAAGLLLMG WQKFTQQRPH APTDYMEALQ TDGQFDYAAS LVKSLASLLV VTSGSAIGRE
     GAMILLAALA ASCFAQRFTP RQEWKLWIAC GAAAGMAAAY RAPLAGSLFI AEVLFGTMML
     ASLGPVIISA VVALLISNLI NHSDALLYSV QLSVTVQARD YALIISTGVL AGLCGPLLLT
     LMNACHRGFV SLKLAPPWQL ALGGLIVGLL SLFTPAVWGN GYSTVQSFLT APPLLMIIAG
     IFLCKLCAVL ASSGSGAPGG VFTPTLFIGL AIGMLYGRSL GLWLPDGEEI TLLLGLTGMA
     TLLAATTHAP IMSTLMICEM TGEYQLLPGL LIACVIASVI SRTLHRDSIY RQHTAKHS
 
 
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