ID V4GRC4_9EURY Unreviewed; 118 AA.
AC V4GRC4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=K933_13212 {ECO:0000313|EMBL:ESP87606.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP87606.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP87606.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP87606.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain G22,
RT Isolated from the Hypersaline Waters of Lake Tyrrell, Australia.";
RL Genome Announc. 1:e01001-13(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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:ESP87606.1}.
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DR EMBL; ASGZ01000055; ESP87606.1; -; Genomic_DNA.
DR RefSeq; WP_023395217.1; NZ_ASGZ01000055.1.
DR AlphaFoldDB; V4GRC4; -.
DR STRING; 1324957.K933_13212; -.
DR PATRIC; fig|1324957.4.peg.2680; -.
DR eggNOG; arCOG04701; Archaea.
DR OrthoDB; 253428at2157; -.
DR Proteomes; UP000017840; 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:0140114; P:cellular detoxification of fluoride; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00454; CrcB; 1.
DR InterPro; IPR003691; FluC.
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}; Ion channel {ECO:0000256|HAMAP-Rule:MF_00454};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00454};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00454};
KW Reference proteome {ECO:0000313|Proteomes:UP000017840};
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 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 118 AA; 11591 MW; 763A501BCC2D2AB6 CRC64;
MREELGAVGV VGVGGAVGAT LRYGAGLAVT GVGGTLLVNV VGSFLLGVLV TRSLPDRVRL
FAATGLCSSF TTYSTFAVET LSLGPRAGAA YVAATYALGV AAAALGTAVG RRTRGAEA
//