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Database: UniProt
Entry: G7M7M8_9CLOT
LinkDB: G7M7M8_9CLOT
Original site: G7M7M8_9CLOT 
ID   G7M7M8_9CLOT            Unreviewed;       125 AA.
AC   G7M7M8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=CDLVIII_5954 {ECO:0000313|EMBL:EHJ02417.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ02417.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHJ02417.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ02417.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHJ02417.1; -; Genomic_DNA.
DR   RefSeq; WP_009173053.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7M7M8; -.
DR   STRING; 641107.CDLVIII_5954; -.
DR   eggNOG; COG0239; Bacteria.
DR   HOGENOM; CLU_114342_3_0_9; -.
DR   Proteomes; UP000005106; 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   Reference proteome {ECO:0000313|Proteomes:UP000005106};
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        5..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        67..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        97..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         75
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         78
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ   SEQUENCE   125 AA;  13325 MW;  BD5EE97CA3931A14 CRC64;
     MQKIIYVGIG GCIGAILRYI VTMQSAKMMN SSLPIGTLIV NVVGGFLIGM IAELSMSTDL
     ISPNLKLFLT TGIMGGLTTF STFSLETITL MSDGRYILGM LNVCLNVFLS LGGVVLARLL
     CRVIV
//
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