ID   MFS55_MYCBT             Reviewed;         518 AA.
AC   C1AN55;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Probable triacylglyceride transporter JTY_1446 {ECO:0000250|UniProtKB:P9WJY3};
DE   AltName: Full=MFS-type drug efflux transporter P55;
GN   OrderedLocusNames=JTY_1446;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
CC   -!- FUNCTION: In association with lipoprotein LprG probably transports
CC       triacylglycerides (TAG) across the inner cell membrane into the
CC       periplasm; TAG probably regulates lipid metabolism and growth
CC       regulation. May be an efflux transporter and involved in maintaining
CC       correct cell wall permeability. Probably required with LprG for normal
CC       surface localization of lipoarabinomannan (LAM).
CC       {ECO:0000250|UniProtKB:P9WJY3}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome fusion
CC       and is one way in which Mycobacteria evade the host immune system.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Triacylglycerides accumulate in lipid droplets in the
CC       cytoplasm of M.tuberculosis stationary phase and dormant bacteria, and
CC       are used as an energy source during starvation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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; AP010918; BAH25734.1; -; Genomic_DNA.
DR   RefSeq; WP_003407310.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AN55; -.
DR   SMR; C1AN55; -.
DR   GeneID; 45425388; -.
DR   KEGG; mbt:JTY_1446; -.
DR   HOGENOM; CLU_000960_2_5_11; -.
DR   OMA; AGYWMTP; -.
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   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..518
FT                   /note="Probable triacylglyceride transporter JTY_1446"
FT                   /id="PRO_0000391005"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   518 AA;  54689 MW;  3D211E3F5A3F77D0 CRC64;
     MRAGRRVAIS AGSLAVLLGA LDTYVVVTIM RDIMNSVGIP INQLHRITWI VTMYLLGYIA
     AMPLLGRASD RFGRKLMLQV SLAGFIIGSV VTALAGHFGD FHMLIAGRTI QGVASGALLP
     ITLALGADLW SQRNRAGVLG GIGAAQELGS VLGPLYGIFI VWLLHDWRDV FWINVPLTAI
     AMVMIHFSLP SHDRSTEPER VDLVGGLLLA LALGLAVIGL YNPNPDGKHV LPDYGAPLLV
     GALVAAVAFF GWERFARTRL IDPAGVHFRP FLSALGASVA AGAALMVTLV DVELFGQGVL
     QMDQAQAAGM LLWFLIALPI GAVTGGWIAT RAGDRAVAFA GLLIAAYGYW LISHWPVDLL
     ADRHNILGLF TVPAMHTDLV VAGLGLGLVI GPLSSATLRV VPSAQHGIAS AAVVVARMTG
     MLIGVAALSA WGLYRFNQIL AGLSAAIPPN ASLLERAAAI GARYQQAFAL MYGEIFTITA
     IVCVFGAVLG LLISGRKEHA DEPEVQEQPT LAPQVEPL