FLQE3_MYCTU
ID FLQE3_MYCTU Reviewed; 237 AA.
AC P9WJB1; L0TAC5; O07189; Q7D6S0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Fluoroquinolones export permease protein Rv2687c;
GN OrderedLocusNames=Rv2687c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN FLUOROQUINOLONES EXPORT, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15273144; DOI=10.1128/aac.48.8.3175-3178.2004;
RA Pasca M.R., Guglierame P., Arcesi F., Bellinzoni M., De Rossi E.,
RA Riccardi G.;
RT "Rv2686c-Rv2687c-Rv2688c, an ABC fluoroquinolone efflux pump in
RT Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 48:3175-3178(2004).
CC -!- FUNCTION: Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c
CC involved in fluoroquinolones export. Confers resistance to
CC ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and
CC sparfloxacin. Probably responsible for the translocation of the
CC substrate across the membrane. {ECO:0000269|PubMed:15273144}.
CC -!- SUBUNIT: The complex is composed of 2 ATP-binding proteins (Rv2688c)
CC and 2 transmembrane proteins (Rv2686c and Rv2687c).
CC {ECO:0000305|PubMed:15273144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AL123456; CCP45485.1; -; Genomic_DNA.
DR PIR; B70529; B70529.
DR RefSeq; NP_217203.1; NC_000962.3.
DR RefSeq; WP_003413912.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; P9WJB1; -.
DR STRING; 83332.Rv2687c; -.
DR PaxDb; P9WJB1; -.
DR DNASU; 888446; -.
DR GeneID; 888446; -.
DR KEGG; mtu:Rv2687c; -.
DR TubercuList; Rv2687c; -.
DR eggNOG; COG1668; Bacteria.
DR OMA; FMFVGTE; -.
DR PhylomeDB; P9WJB1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IMP:MTBBASE.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..237
FT /note="Fluoroquinolones export permease protein Rv2687c"
FT /id="PRO_0000390880"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 237 AA; 25576 MW; 9A240CD234B4631E CRC64;
MTRLVPALRL ELTLQVRQKF LHAAVFSGLI WLAVLLPMPV SLRPVAEPYV LVGDIAIIGF
FFVGGTVFFE KQERTIGAIV STPLRFWEYL AAKLTVLLAI SLFVAVVVAT IVHGLGYHLL
PLVAGIVLGT LLMLLVGFSS SLPFASVTDW FLAAVIPLAI MLAPPVVHYS GLWPNPVLYL
IPTQGPLLLL GAAFDQVSLA PWQVGYAVVY PIVCAAGLCR AAKALFGRYV VQRSGVL