ID   FLQE1_MYCTU             Reviewed;         301 AA.
AC   P9WQL7; L0TAL1; O07190; Q8VJE4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Fluoroquinolones export ATP-binding protein Rv2688c;
DE            EC=7.6.2.-;
GN   OrderedLocusNames=Rv2688c;
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, ACTIVITY REGULATION, 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 energy coupling to the transport
CC       system. {ECO:0000269|PubMed:15273144}.
CC   -!- ACTIVITY REGULATION: Inhibited by reserpine and verapamil.
CC       {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:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45486.1; -; Genomic_DNA.
DR   PIR; C70529; C70529.
DR   RefSeq; NP_217204.1; NC_000962.3.
DR   RefSeq; WP_003917051.1; NZ_NVQJ01000017.1.
DR   AlphaFoldDB; P9WQL7; -.
DR   SMR; P9WQL7; -.
DR   STRING; 83332.Rv2688c; -.
DR   PaxDb; P9WQL7; -.
DR   DNASU; 888463; -.
DR   GeneID; 888463; -.
DR   KEGG; mtu:Rv2688c; -.
DR   TubercuList; Rv2688c; -.
DR   eggNOG; COG1131; Bacteria.
DR   OMA; FIYEMGG; -.
DR   PhylomeDB; P9WQL7; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:MTBBASE.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:MTBBASE.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..301
FT                   /note="Fluoroquinolones export ATP-binding protein Rv2688c"
FT                   /id="PRO_0000390878"
FT   DOMAIN          18..246
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         52..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   301 AA;  33100 MW;  A21E35CC376FB4E6 CRC64;
     MTALNRAVAS ARVGTEVIRV RGLTFRYPKA AEPAVRGMEF TVGRGEIFGL LGPSGAGKST
     TQKLLIGLLR DHGGQATVWD KEPAEWGPDY YERIGVSFEL PNHYQKLTGY ENLRFFASLY
     AGATADPMQL LAAVGLADDA HTLVGKYSKG MQMRLPFARS LINDPELLFL DEPTSGLDPV
     NARKIKDIIV DLKARGRTIF LTTHDMATAD ELCDRVAFVV DGRIVALDSP TELKIARSRR
     RVRVEYRGDG GGLETAEFGM DGLADDPAFH SVLRNHHVET IHSREASLDD VFVEVTGRQL
     T