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Database: UniProt
Entry: Q9CCP7
LinkDB: Q9CCP7
Original site: Q9CCP7 
ID   MFS55_MYCLE             Reviewed;         509 AA.
AC   Q9CCP7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Probable triacylglyceride transporter ML0556 {ECO:0000250|UniProtKB:P9WJY3};
DE   AltName: Full=MFS-type drug efflux transporter P55;
GN   OrderedLocusNames=ML0556;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
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.leprae, and are used as an energy source during
CC       starvation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL583918; CAC30064.1; -; Genomic_DNA.
DR   PIR; D86978; D86978.
DR   RefSeq; NP_301470.1; NC_002677.1.
DR   RefSeq; WP_010907794.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCP7; -.
DR   SMR; Q9CCP7; -.
DR   STRING; 272631.gene:17574377; -.
DR   KEGG; mle:ML0556; -.
DR   PATRIC; fig|272631.5.peg.967; -.
DR   Leproma; ML0556; -.
DR   eggNOG; COG0477; Bacteria.
DR   HOGENOM; CLU_000960_2_5_11; -.
DR   OrthoDB; 3453194at2; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd17321; MFS_MMR_MDR_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   PANTHER; PTHR23501:SF202; TRIACYLGLYCERIDE TRANSPORTER RV1410C-RELATED; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..509
FT                   /note="Probable triacylglyceride transporter ML0556"
FT                   /id="PRO_0000434647"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   509 AA;  53712 MW;  2EC18FF618051644 CRC64;
     MSTRAGRRVA ISAGSLAVLL GALDTYVVVT IMRDIMHDVG IPVNQMQRIT WIVTMYLLGY
     IAAMPLLSRA SDRFGRKLLL QVSLAGFAIG SVMTALAGQF GDFHMLIAGR TIQGVASGAL
     LPITLALGAD LWAQRNRAGV LGGIGAAQEL GSVLGPLYGI FIVWLFSDWR YVFWINIPLT
     AIAMLMIQVS LSAHDRGDEL EKVDVVGGVL LAIALGLVVI GLYNPQPDSK QVLPSYGVPV
     LVGGIVATVA FAVWERCART RLIDPAGVHI RPFLSALGAS VAAGAALMVT LVNVELFGQG
     VLGMDQTQAA GLLVWFLIAL PIGAVLGGWG ATKAGDRTMT FVGLLITAGG YWLISHWPVD
     LLNYRRSIFG LFSVPTMYAD LLVAGLGLGL VIGPLSSATL RVVPTAQHGI ASAAVVVARM
     TGMLIGVAAL TAWGLYRFNQ ILAGLSTAVP PDATLIERAA AVADQAKRAY TMMYSDIFMI
     TAIVCVIGAL LGLLISSRKE HASEPKVPE
//
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