ID E8PJV4_THESS Unreviewed; 127 AA.
AC E8PJV4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN Name=crcB {ECO:0000256|HAMAP-Rule:MF_00454,
GN ECO:0000313|EMBL:ADW20806.1};
GN Synonyms=fluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN OrderedLocusNames=TSC_c01600 {ECO:0000313|EMBL:ADW20806.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW20806.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW20806.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
CC -!- FUNCTION: Fluoride-specific ion channel. Important for reducing
CC fluoride concentration in the cell, thus reducing its toxicity.
CC {ECO:0000256|HAMAP-Rule:MF_00454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159,
CC ChEBI:CHEBI:17051; Evidence={ECO:0000256|ARBA:ARBA00035585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160;
CC Evidence={ECO:0000256|ARBA:ARBA00035585};
CC -!- ACTIVITY REGULATION: Na(+) is not transported, but it plays an
CC essential structural role and its presence is essential for fluoride
CC channel function. {ECO:0000256|HAMAP-Rule:MF_00454}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00454};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00454}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43)
CC family. {ECO:0000256|ARBA:ARBA00035120, ECO:0000256|HAMAP-
CC Rule:MF_00454}.
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DR EMBL; CP001962; ADW20806.1; -; Genomic_DNA.
DR AlphaFoldDB; E8PJV4; -.
DR STRING; 743525.TSC_c01600; -.
DR KEGG; tsc:TSC_c01600; -.
DR eggNOG; COG0239; Bacteria.
DR HOGENOM; CLU_114342_2_3_0; -.
DR Proteomes; UP000008087; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0062054; F:fluoride channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140114; P:cellular detoxification of fluoride; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00454; CrcB; 1.
DR InterPro; IPR003691; FluC.
DR NCBIfam; TIGR00494; crcB; 1.
DR PANTHER; PTHR28259; FLUORIDE EXPORT PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR28259:SF1; FLUORIDE EXPORT PROTEIN 1-RELATED; 1.
DR Pfam; PF02537; CRCB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00454};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|HAMAP-
KW Rule:MF_00454}; Ion transport {ECO:0000256|HAMAP-Rule:MF_00454};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00454};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00454};
KW Sodium {ECO:0000256|HAMAP-Rule:MF_00454};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00454};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00454}; Transport {ECO:0000256|HAMAP-Rule:MF_00454}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 76
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 79
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 127 AA; 13388 MW; F5DC41CC1B688E3F CRC64;
MGVERYLLVA LGGALGSALR YGLGAWVQAL TGPSFPYSTL LINALGSFLI GVVIRLSLEG
ALSGEGRLFL AVGVLGGFTT FSTFSYETLA LIQDGEAWRA FLYVVFSVFL GLFLVLLGYR
LGGALVA
//
