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Database: UniProt
Entry: A0A060M6L6_9BACI
LinkDB: A0A060M6L6_9BACI
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ID   A0A060M6L6_9BACI        Unreviewed;       118 AA.
AC   A0A060M6L6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN   Name=fluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN   Synonyms=crcB {ECO:0000256|HAMAP-Rule:MF_00454};
GN   ORFNames=BleG1_3181 {ECO:0000313|EMBL:AIC95744.1};
OS   Shouchella lehensis G1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95744.1, ECO:0000313|Proteomes:UP000027142};
RN   [1] {ECO:0000313|EMBL:AIC95744.1, ECO:0000313|Proteomes:UP000027142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:AIC95744.1,
RC   ECO:0000313|Proteomes:UP000027142};
RX   PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA   Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA   Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA   Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT   "A comparative genomic analysis of the alkalitolerant soil bacterium
RT   Bacillus lehensis G1.";
RL   Gene 545:253-261(2014).
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; CP003923; AIC95744.1; -; Genomic_DNA.
DR   RefSeq; WP_038483003.1; NZ_CP003923.1.
DR   AlphaFoldDB; A0A060M6L6; -.
DR   STRING; 1246626.BleG1_3181; -.
DR   KEGG; ble:BleG1_3181; -.
DR   PATRIC; fig|1246626.3.peg.3171; -.
DR   eggNOG; COG0239; Bacteria.
DR   HOGENOM; CLU_114342_3_2_9; -.
DR   OrthoDB; 9815830at2; -.
DR   Proteomes; UP000027142; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000027142};
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        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        35..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         71
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         74
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ   SEQUENCE   118 AA;  12805 MW;  04EC63585708AC22 CRC64;
     MLTTLLLVSI GGGTGAFLRF IIGEFLTLHY KWSRCFTVIA FINIVGSTVL GVAVAAKPSS
     VFELFILYLC GGFTTFSTFS LEALQGFLDK EWIKGISYII VTVIGSMLGF GLGFVILF
//
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