CHLEP_MYCTU
ID CHLEP_MYCTU Reviewed; 413 AA.
AC P9WJX7; L0T4M5; O07435; Q7DAA8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Chloramphenicol efflux pump Rv0191 {ECO:0000305};
GN OrderedLocusNames=Rv0191;
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, AND ACTIVITY REGULATION.
RC STRAIN=H37Ra;
RX PubMed=28584158; DOI=10.1128/aac.00940-17;
RA Zhang Y., Zhang J., Cui P., Zhang Y., Zhang W.;
RT "Identification of novel efflux proteins Rv0191, Rv3756c, Rv3008, and
RT Rv1667c involved in pyrazinamide resistance in Mycobacterium
RT tuberculosis.";
RL Antimicrob. Agents Chemother. 61:E00940-E00940(2017).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=31054279; DOI=10.1016/j.abb.2019.04.010;
RA Li X., Li P., Ruan C., Xie L.X., Gu Y., Li J., Yi Q., Lv X., Xie J.;
RT "Mycobacterium tuberculosis Rv0191 is an efflux pump of major facilitator
RT superfamily transporter regulated by Rv1353c.";
RL Arch. Biochem. Biophys. 667:59-66(2019).
CC -!- FUNCTION: Active efflux pump that plays an important role in
CC chloramphenicol resistance (PubMed:31054279). Overexpression causes
CC pyrazinamide resistance (PubMed:28584158).
CC {ECO:0000269|PubMed:28584158, ECO:0000269|PubMed:31054279}.
CC -!- ACTIVITY REGULATION: Inhibited by the drug efflux pump inhibitors
CC verapamil, resperine, piperine, chlorpromazine and carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:28584158,
CC ECO:0000269|PubMed:31054279}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is negatively regulated by the transcriptional
CC repressor Rv1353c. {ECO:0000269|PubMed:31054279}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42918.1; -; Genomic_DNA.
DR PIR; B70907; B70907.
DR RefSeq; NP_214705.1; NC_000962.3.
DR RefSeq; WP_003401149.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P9WJX7; -.
DR SMR; P9WJX7; -.
DR STRING; 83332.Rv0191; -.
DR PaxDb; P9WJX7; -.
DR DNASU; 886770; -.
DR GeneID; 45424162; -.
DR GeneID; 886770; -.
DR KEGG; mtu:Rv0191; -.
DR TubercuList; Rv0191; -.
DR eggNOG; COG2814; Bacteria.
DR OMA; SAHFTAY; -.
DR PhylomeDB; P9WJX7; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..413
FT /note="Chloramphenicol efflux pump Rv0191"
FT /id="PRO_0000390681"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 42911 MW; F22DB64E81C0822B CRC64;
MTAPTGTSAT TTRPWTPRIA TQLSVLACAA FIYVTAEILP VGALSAIARN LRVSVVLVGT
LLSWYALVAA VTTVPLVRWT AHWPRRRALV VSLVCLTVSQ LVSALAPNFA VLAAGRVLCA
VTHGLLWAVI APIATRLVPP SHAGRATTSI YIGTSLALVV GSPLTAAMSL MWGWRLAAVC
VTGAAAAVAL AARLALPEMV LRADQLEHVG RRARHHRNPR LVKVSVLTMI AVTGHFVSYT
YIVVIIRDVV GVRGPNLAWL LAAYGVAGLV SVPLVARPLD RWPKGAVIVG MTGLTAAFTL
LTALAFGERH TAATALLGTG AIVLWGALAT AVSPMLQSAA MRSGGDDPDG ASGLYVTAFQ
IGIMAGALLG GLLYERSLAM MLTASAGLMG VALFGMTVSQ HLFENPTLSP GDG
