ID   STP_MYCTU               Reviewed;         537 AA.
AC   P9WG91; L0TC78; O08222; P71879; Q7D7B2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Multidrug resistance protein Stp;
DE   AltName: Full=Spectinomycin tetracycline efflux pump;
GN   Name=stp; OrderedLocusNames=Rv2333c;
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 ANTIBIOTIC RESISTANCE.
RX   PubMed=17242035; DOI=10.1093/jac/dkl510;
RA   Ramon-Garcia S., Martin C., De Rossi E., Ainsa J.A.;
RT   "Contribution of the Rv2333c efflux pump (the Stp protein) from
RT   Mycobacterium tuberculosis to intrinsic antibiotic resistance in
RT   Mycobacterium bovis BCG.";
RL   J. Antimicrob. Chemother. 59:544-547(2007).
CC   -!- FUNCTION: Contributes to spectinomycin and tetracycline resistance.
CC       {ECO:0000269|PubMed:17242035}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45121.1; -; Genomic_DNA.
DR   PIR; F70705; F70705.
DR   RefSeq; NP_216849.1; NC_000962.3.
DR   RefSeq; WP_003906797.1; NZ_NVQJ01000012.1.
DR   AlphaFoldDB; P9WG91; -.
DR   SMR; P9WG91; -.
DR   STRING; 83332.Rv2333c; -.
DR   PaxDb; P9WG91; -.
DR   DNASU; 887274; -.
DR   GeneID; 887274; -.
DR   KEGG; mtu:Rv2333c; -.
DR   TubercuList; Rv2333c; -.
DR   eggNOG; COG0477; Bacteria.
DR   OMA; TALFMEN; -.
DR   PhylomeDB; P9WG91; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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; -; 1.
DR   InterPro; IPR004638; EmrB-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..537
FT                   /note="Multidrug resistance protein Stp"
FT                   /id="PRO_0000390886"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   537 AA;  57115 MW;  237A9423637858B0 CRC64;
     MNRTQLLTLI ATGLGLFMIF LDALIVNVAL PDIQRSFAVG EDGLQWVVAS YSLGMAVFIM
     SAATLADLDG RRRWYLIGVS LFTLGSIACG LAPSIAVLTT ARGAQGLGAA AVSVTSLALV
     SAAFPEAKEK ARAIGIWTAI ASIGTTTGPT LGGLLVDQWG WRSIFYVNLP MGALVLFLTL
     CYVEESCNER ARRFDLSGQL LFIVAVGALV YAVIEGPQIG WTSVQTIVML WTAAVGCALF
     VWLERRSSNP MMDLTLFRDT SYALAIATIC TVFFAVYGML LLTTQFLQNV RGYTPSVTGL
     MILPFSAAVA IVSPLVGHLV GRIGARVPIL AGLCMLMLGL LMLIFSEHRS SALVLVGLGL
     CGSGVALCLT PITTVAMTAV PAERAGMASG IMSAQRAIGS TIGFAVLGSV LAAWLSATLE
     PHLERAVPDP VQRHVLAEII IDSANPRAHV GGIVPRRHIE HRDPVAIAEE DFIEGIRVAL
     LVATATLAVV FLAGWRWFPR DVHTAGSDLS ERLPTAMTVE CAVSHMPGAT WCRLWPA