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Database: UniProt
Entry: A0A1Q9HNX3_9VIBR
LinkDB: A0A1Q9HNX3_9VIBR
Original site: A0A1Q9HNX3_9VIBR 
ID   A0A1Q9HNX3_9VIBR        Unreviewed;       127 AA.
AC   A0A1Q9HNX3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:KAB1460365.1};
GN   Synonyms=fluC {ECO:0000256|HAMAP-Rule:MF_00454};
GN   ORFNames=BIY22_15770 {ECO:0000313|EMBL:OLQ92501.1}, F7O85_00970
GN   {ECO:0000313|EMBL:KAB1460365.1};
OS   Vibrio panuliri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ92501.1, ECO:0000313|Proteomes:UP000186313};
RN   [1] {ECO:0000313|EMBL:OLQ92501.1, ECO:0000313|Proteomes:UP000186313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ92501.1,
RC   ECO:0000313|Proteomes:UP000186313};
RA   Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAB1460365.1, ECO:0000313|Proteomes:UP000446972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1460365.1,
RC   ECO:0000313|Proteomes:UP000446972};
RA   Das S.S.;
RT   "Whole genome sequence of Vibrio panuliri LBS 2.";
RL   Submitted (SEP-2019) 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:OLQ92501.1}.
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DR   EMBL; WAHU01000004; KAB1460365.1; -; Genomic_DNA.
DR   EMBL; MJMJ01000003; OLQ92501.1; -; Genomic_DNA.
DR   RefSeq; WP_075706429.1; NZ_WAHU01000004.1.
DR   AlphaFoldDB; A0A1Q9HNX3; -.
DR   STRING; 1381081.BIY22_15770; -.
DR   OrthoDB; 9806299at2; -.
DR   Proteomes; UP000186313; Unassembled WGS sequence.
DR   Proteomes; UP000446972; 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   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        41..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        71..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT   TRANSMEM        106..125
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   127 AA;  13673 MW;  CCB4C0E559AC2057 CRC64;
     MGQLSILGFI ALGGAFGACS RYLVSELCVT LLGRGFPYGT LTVNVVGSFI MGLLIAAFES
     EIMSIEPWRQ IIGLGFLGAL TTFSTFSMDN VLLMQQGAFF KMGLNVLLNV FLSISAAWLG
     FQLLMKS
//
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