ID CLCB_SHIFL Reviewed; 418 AA.
AC P59638;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 24-JAN-2024, entry version 119.
DE RecName: Full=Voltage-gated ClC-type chloride channel ClcB;
GN Name=clcB; OrderedLocusNames=SF1613, S1745;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAN43197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP17085.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43197.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17085.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_707490.3; NC_004337.2.
DR AlphaFoldDB; P59638; -.
DR SMR; P59638; -.
DR STRING; 198214.SF1613; -.
DR PaxDb; 198214-SF1613; -.
DR GeneID; 1024819; -.
DR KEGG; sfl:SF1613; -.
DR KEGG; sft:NCTC1_01750; -.
DR KEGG; sfx:S1745; -.
DR PATRIC; fig|198214.7.peg.1906; -.
DR HOGENOM; CLU_015263_5_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0010447; P:response to acidic pH; IEA:InterPro.
DR CDD; cd00400; Voltage_gated_ClC; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
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 PANTHER; PTHR43427; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR PANTHER; PTHR43427:SF6; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chloride; Chloride channel;
KW Ion channel; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..418
FT /note="Voltage-gated ClC-type chloride channel ClcB"
FT /id="PRO_0000094490"
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..172
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..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; 44277 MW; BEED5EA651D470CA CRC64;
MFRRLLIATV VGILAVFAVA GFRHAMLLLE WLFLNNDSGS LVNAATNLSS WRRLLTPALG
GLAAGLLLMG WQKFTQQRPH APTDYMEALQ TDGQFDYAAS LVKSLASLLV VTSGSAIGRE
GAMILLAALA ASCFAQRFTP RQEWKLWIAC GAAAGMAAAY RAPLAGSLFI AEVLFGTMML
ASLGPVIISA IVAWLVSNLI NHSDALLYNV QLSVTVQARD YALIISTGVL AGLCGPLLLT
LMNACHRGFV SLKLAPPWQL ALGGLIVGLL SLFTPAVWGN GYSTVQSFLT APPLLMIIAG
IFLCKLCAVL ASSGSGAPGG VFTPTLFIGL AIGMLYGRSL GLWFPDGEEI TLLLGLTGMA
TLLAATTHAP IMSTLMICEM TGEYQLLPGL LIACVIASVI SRTLHRDSIY RQHTAQHS
//
