ID L0AH96_NATGS Unreviewed; 137 AA.
AC L0AH96;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=Natgr_1226 {ECO:0000313|EMBL:AFZ72450.1};
GN ORFNames=C490_00090 {ECO:0000313|EMBL:ELY74321.1}, CYV19_03760
GN {ECO:0000313|EMBL:PLK21424.1};
OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS 104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronobacterium.
OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ72450.1, ECO:0000313|Proteomes:UP000010468};
RN [1] {ECO:0000313|Proteomes:UP000010468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC {ECO:0000313|Proteomes:UP000010468};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFZ72450.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ72450.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY74321.1, ECO:0000313|Proteomes:UP000011613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:ELY74321.1,
RC ECO:0000313|Proteomes:UP000011613};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:PLK21424.1, ECO:0000313|Proteomes:UP000234484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:PLK21424.1,
RC ECO:0000313|Proteomes:UP000234484};
RC TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21424.1};
RA Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA Huang J.;
RT "The characterization of oligonucleotides binding to NgAgo.";
RL Submitted (DEC-2017) 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 -!- 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}.
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DR EMBL; CP003377; AFZ72450.1; -; Genomic_DNA.
DR EMBL; AOIC01000003; ELY74321.1; -; Genomic_DNA.
DR EMBL; PKKI01000008; PLK21424.1; -; Genomic_DNA.
DR RefSeq; WP_005575393.1; NZ_PKKI01000008.1.
DR AlphaFoldDB; L0AH96; -.
DR STRING; 797304.Natgr_1226; -.
DR GeneID; 14207094; -.
DR KEGG; nge:Natgr_1226; -.
DR PATRIC; fig|797304.7.peg.18; -.
DR eggNOG; arCOG04701; Archaea.
DR HOGENOM; CLU_114342_1_4_2; -.
DR Proteomes; UP000010468; Chromosome.
DR Proteomes; UP000011613; Unassembled WGS sequence.
DR Proteomes; UP000234484; 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:UP000010468};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 137 AA; 14162 MW; A9CFC38D3B4158AA CRC64;
MATDHPLVRL ETLALIAIGG FAGSNLRFFA VELFAAVPAV LLVNVLGSFA LGFLVYEAEY
AGLVGKQSRI VFTTGFLSSL TTYSTFAVQT ATAADPMLVL AIVAANYGIG FTAVIASRSV
ARRVTAGVRS SPGGETA
//
