MFS55_MYCBO
ID MFS55_MYCBO Reviewed; 518 AA.
AC Q7U042; A0A1R3XYB0; X2BI12;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Probable triacylglyceride transporter Mb1445c {ECO:0000250|UniProtKB:P9WJY3};
DE AltName: Full=MFS-type drug efflux transporter P55;
GN OrderedLocusNames=BQ2027_MB1445C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=BCG;
RX PubMed=11181364; DOI=10.1128/aac.45.3.800-804.2001;
RA Silva P.E., Bigi F., Santangelo M.P., Romano M.I., Martin C., Cataldi A.,
RA Ainsa J.A.;
RT "Characterization of P55, a multidrug efflux pump in Mycobacterium bovis
RT and Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 45:800-804(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 (By similarity). Confers resistance to tetracycline and
CC aminoglycosides such as streptomycin and gentamicin (PubMed:11181364).
CC Probably an efflux transporter, involved in maintaining correct cell
CC wall permeability. Probably required with LprG for normal surface
CC localization of lipoarabinomannan (LAM). {ECO:0000250|UniProtKB:P9WJY3,
CC ECO:0000269|PubMed:11181364}.
CC -!- ACTIVITY REGULATION: Inhibited by CCCP, verapamil and reserpine.
CC {ECO:0000269|PubMed:11181364}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:11181364}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11181364}.
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}.
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DR EMBL; LT708304; SIU00048.1; -; Genomic_DNA.
DR RefSeq; NP_855097.1; NC_002945.3.
DR RefSeq; WP_003407310.1; NC_002945.4.
DR AlphaFoldDB; Q7U042; -.
DR SMR; Q7U042; -.
DR EnsemblBacteria; SIU00048; SIU00048; BQ2027_MB1445C.
DR GeneID; 45425388; -.
DR PATRIC; fig|233413.5.peg.1580; -.
DR OMA; AGYWMTP; -.
DR Proteomes; UP000001419; 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; -; 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 Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Probable triacylglyceride transporter Mb1445c"
FT /id="PRO_0000391003"
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
