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Database: UniProt
Entry: A0A0K9H8H8_9BACI
LinkDB: A0A0K9H8H8_9BACI
Original site: A0A0K9H8H8_9BACI 
ID   A0A0K9H8H8_9BACI        Unreviewed;       128 AA.
AC   A0A0K9H8H8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AC623_16150 {ECO:0000313|EMBL:KMY55274.1};
OS   Bacillus sp. FJAT-27231.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY55274.1, ECO:0000313|Proteomes:UP000037077};
RN   [1] {ECO:0000313|Proteomes:UP000037077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
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:KMY55274.1}.
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DR   EMBL; LFZU01000001; KMY55274.1; -; Genomic_DNA.
DR   RefSeq; WP_049664336.1; NZ_LFZU01000001.1.
DR   AlphaFoldDB; A0A0K9H8H8; -.
DR   STRING; 1679168.AC623_16150; -.
DR   PATRIC; fig|1679168.3.peg.3455; -.
DR   OrthoDB; 9799631at2; -.
DR   Proteomes; UP000037077; 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: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:UP000037077};
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        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        62..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        92..111
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   128 AA;  14096 MW;  70B875B553138E7D CRC64;
     MNVLFVMIGG FFGAIGRYLA GEWVQPVHEF PLGTLLINLI GCFFLGWFLT FVNRYKRVKP
     EITLMIGTGV IGSFTTFSTF SVETVHLFQG GHAFLAVLYV LVSTLFGLLL ADAGRRWALS
     GEKEGVKG
//
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