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Database: UniProt
Entry: W4QG15_9BACI
LinkDB: W4QG15_9BACI
Original site: W4QG15_9BACI 
ID   W4QG15_9BACI            Unreviewed;       126 AA.
AC   W4QG15;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=JCM9152_2292 {ECO:0000313|EMBL:GAE30867.1};
OS   Halalkalibacter hemicellulosilyticusJCM 9152.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE30867.1, ECO:0000313|Proteomes:UP000018895};
RN   [1] {ECO:0000313|EMBL:GAE30867.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE30867.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(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}.
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:GAE30867.1}.
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DR   EMBL; BAUU01000014; GAE30867.1; -; Genomic_DNA.
DR   RefSeq; WP_035343914.1; NZ_BAZO01000014.1.
DR   AlphaFoldDB; W4QG15; -.
DR   STRING; 1236971.JCM9152_2292; -.
DR   Proteomes; UP000018895; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018895};
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        33..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        68..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        102..124
FT                   /note="Helical"
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"
FT   BINDING         81
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ   SEQUENCE   126 AA;  14359 MW;  A13985ED52A1EE99 CRC64;
     MNLILLAISG ALGAISRYLV GLYMMERFPN PPIPIAMLCV NTIGSFGLGF FFSFYFSQLP
     IGAYEDPYYL FIGIGFFGAF TTFSTYSVEA MQLYKQKKWK ELVLYVSFSI FGSILFFLIG
     FTVFRF
//
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