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Database: UniProt
Entry: C0QTQ0_PERMH
LinkDB: C0QTQ0_PERMH
Original site: C0QTQ0_PERMH 
ID   C0QTQ0_PERMH            Unreviewed;       124 AA.
AC   C0QTQ0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN   Name=crcB {ECO:0000256|HAMAP-Rule:MF_00454,
GN   ECO:0000313|EMBL:ACO04932.1};
GN   Synonyms=fluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN   OrderedLocusNames=PERMA_0270 {ECO:0000313|EMBL:ACO04932.1};
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO04932.1, ECO:0000313|Proteomes:UP000001366};
RN   [1] {ECO:0000313|EMBL:ACO04932.1, ECO:0000313|Proteomes:UP000001366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00454}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00454}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {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}.
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DR   EMBL; CP001230; ACO04932.1; -; Genomic_DNA.
DR   RefSeq; WP_015899036.1; NC_012440.1.
DR   AlphaFoldDB; C0QTQ0; -.
DR   STRING; 123214.PERMA_0270; -.
DR   PaxDb; 123214-PERMA_0270; -.
DR   KEGG; pmx:PERMA_0270; -.
DR   eggNOG; COG0239; Bacteria.
DR   HOGENOM; CLU_114342_3_0_0; -.
DR   OMA; WGTFTVN; -.
DR   OrthoDB; 9815830at2; -.
DR   Proteomes; UP000001366; Chromosome.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00454};
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:UP000001366};
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..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        66..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        102..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         74
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   BINDING         77
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ   SEQUENCE   124 AA;  13669 MW;  11640834A7836018 CRC64;
     MEYIYVMIGG SLGAVSRFFI SNYVNRNLPL DFPAGTLVVN SLGSFILVFF LILSIEKLSI
     DPVWRLFFAV GFLGAFTTFS TFSYETIALF QDGEYTKAML NIILNNVVSI TAGISGLFLA
     RVIG
//
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