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Database: UniProt
Entry: A0A0M0G922_SPOGL
LinkDB: A0A0M0G922_SPOGL
Original site: A0A0M0G922_SPOGL 
ID   A0A0M0G922_SPOGL        Unreviewed;       122 AA.
AC   A0A0M0G922;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AF332_05940 {ECO:0000313|EMBL:KON86405.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON86405.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KON86405.1}.
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DR   EMBL; LGUF01000007; KON86405.1; -; Genomic_DNA.
DR   RefSeq; WP_053433768.1; NZ_LGUF01000007.1.
DR   AlphaFoldDB; A0A0M0G922; -.
DR   STRING; 1459.AF332_05940; -.
DR   PATRIC; fig|1459.3.peg.1251; -.
DR   OrthoDB; 9815830at2; -.
DR   Proteomes; UP000037109; Unassembled WGS sequence.
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:SF16; FLUORIDE ION TRANSPORTER CRCB 2-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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00454}; 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..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        61..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         72
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
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"
SQ   SEQUENCE   122 AA;  13189 MW;  878F5ACF0D908BD2 CRC64;
     MSMFHILLVG IGGLFGAVCR LWVSQIINKR LVSKFPVATL VINLIGSLLL GIMVGSGIDG
     SLFMLLGTGF MGAFTTFSAF KLEAIQLHID KRKKEFLFYN VFSYGGGILL AFLGIELGIL
     LG
//
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