ID Q07MP6_RHOP5 Unreviewed; 145 AA. AC Q07MP6; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 22-FEB-2023, entry version 91. DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000256|HAMAP-Rule:MF_00454}; GN Name=crcB {ECO:0000256|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=RPE_2851 {ECO:0000313|EMBL:ABJ06788.1}; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ06788.1}; RN [1] {ECO:0000313|EMBL:ABJ06788.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ06788.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Important for reducing fluoride concentration in the cell, CC thus reducing its toxicity. {ECO:0000256|ARBA:ARBA00004023, CC 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 CrcB (TC 9.B.71) family. CC {ECO:0000256|ARBA:ARBA00007610, ECO:0000256|HAMAP-Rule:MF_00454}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000463; ABJ06788.1; -; Genomic_DNA. DR AlphaFoldDB; Q07MP6; -. DR STRING; 316055.RPE_2851; -. DR EnsemblBacteria; ABJ06788; ABJ06788; RPE_2851. DR KEGG; rpe:RPE_2851; -. DR eggNOG; COG0239; Bacteria. DR HOGENOM; CLU_114342_3_0_5; -. DR OMA; TWMLETH; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:1903425; F:fluoride transmembrane transporter activity; IEA:UniProt. DR HAMAP; MF_00454; CrcB; 1. DR InterPro; IPR003691; CrcB. 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|ARBA:ARBA00022519}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00454}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00454}. FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 44..67 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 83..100 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 112..136 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" SQ SEQUENCE 145 AA; 15655 MW; 0BDFDC6C5AA01BF2 CRC64; MSGARSELRD RAVLYGYIAA GSVIGGWARY LVSVVQTAWL GPGLGFPWAT LFVNVTGSFV IGFYATLTAP DGRVFASSRQ RQLVMTGICG GYTTFSGFSF ETFELLRTDH ALAALINLGI SPVTWLLAVW IGHFAATRLN RLKGS //