CLCB_ECO24
ID CLCB_ECO24 Reviewed; 418 AA.
AC A7ZM51;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Voltage-gated ClC-type chloride channel ClcB {ECO:0000255|HAMAP-Rule:MF_01203};
GN Name=clcB {ECO:0000255|HAMAP-Rule:MF_01203};
GN OrderedLocusNames=EcE24377A_1800;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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:0000255|HAMAP-
CC Rule:MF_01203}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01203}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01203}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01203}.
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DR EMBL; CP000800; ABV17150.1; -; Genomic_DNA.
DR AlphaFoldDB; A7ZM51; -.
DR SMR; A7ZM51; -.
DR EnsemblBacteria; ABV17150; ABV17150; EcE24377A_1800.
DR KEGG; ecw:EcE24377A_1800; -.
DR HOGENOM; CLU_015263_5_2_6; -.
DR OMA; GPLTMTF; -.
DR Proteomes; UP000001122; 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_1000066131"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01203"
SQ SEQUENCE 418 AA; 44172 MW; 888E781093E33A4A CRC64;
MFRRLLIATV VGILAAFAVA GFRHAMLLLE WLFLNNDSGS LVNAATNLSP WRRLLTPALG
GLAAGLLLMG WQKFTQQRPH APTDYMEALQ TDGQFDYAAS LVKSLASLLV VTSGSAIGRE
GAMILLAALA ASCFAQRFTP RQEWKLWIAC GAAAGMAAAY RAPLAGSLFI AEVLFGTMML
ASLGPVIISA VVALLVSNLI NHSDALLYNV QLSVTVQARD YALIISTGVL AGLCGPLLLT
LMNACHRGFV SLKLAPPWQL ALGGLIVGLL SLFTPAVWGN GYSTVQSFLT APPLLMIIAG
IFLCKLCAVL ASSGSGAPGG VFTPTLFIGL AIGMLYGRSL GLWFPDGEEI TLLLGLTGMA
TLLAATTHAP IMSTLMICEM TGEYQLLPGL LIACVIASVI SRTLHRDSIY RQHTAQHS