MFS55_MYCBP
ID MFS55_MYCBP Reviewed; 518 AA.
AC A1KIJ9;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Probable triacylglyceride transporter BCG_1471c {ECO:0000250|UniProtKB:P9WJY3};
DE AltName: Full=MFS-type drug efflux transporter P55;
GN OrderedLocusNames=BCG_1471c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP FUNCTION IN ANTIBIOTIC RESISTANCE, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=BCG / Pasteur 1173;
RX PubMed=19564371; DOI=10.1128/aac.00550-09;
RA Ramon-Garcia S., Martin C., Thompson C.J., Ainsa J.A.;
RT "Role of the Mycobacterium tuberculosis P55 efflux pump in intrinsic drug
RT resistance, oxidative stress responses, and growth.";
RL Antimicrob. Agents Chemother. 53:3675-3682(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=BCG / Pasteur 1173;
RX PubMed=26155739; DOI=10.1080/21505594.2015.1044195;
RA Ramon-Garcia S., Stewart G.R., Hui Z.K., Mohn W.W., Thompson C.J.;
RT "The mycobacterial P55 efflux pump is required for optimal growth on
RT cholesterol.";
RL Virulence 6:444-448(2015).
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 several drugs such as
CC rifampicin, clofazimine and novobiocin; is also part of the oxidative
CC stress response and is needed to maintain normal growth characteristics
CC (PubMed:19564371). Probably an efflux transporter, involved in
CC maintaining correct cell wall permeability. Probably required with LprG
CC for normal surface localization of lipoarabinomannan (LAM) (By
CC similarity). Required for optimal growth on cholesterol
CC (PubMed:26155739). {ECO:0000250|UniProtKB:P9WJY3,
CC ECO:0000269|PubMed:19564371, ECO:0000269|PubMed:26155739}.
CC -!- ACTIVITY REGULATION: Inhibited by CCCP and valinomycin.
CC {ECO:0000269|PubMed:19564371}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to a number of
CC antibiotics such as rifampicin, clofazimine, novobiocin, ethambutol and
CC vancomycin; grows slowly in liquid culture and forms small colonies
CC (PubMed:19564371). Severely reduced growth with cholesterol as the sole
CC carbon source; lag phase is very long and grows much slower
CC (PubMed:26155739). Accumulates less intracellular cholesterol
CC (PubMed:26155739). {ECO:0000269|PubMed:19564371,
CC ECO:0000269|PubMed:26155739}.
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; AM408590; CAL71458.1; -; Genomic_DNA.
DR RefSeq; WP_003407310.1; NC_008769.1.
DR AlphaFoldDB; A1KIJ9; -.
DR SMR; A1KIJ9; -.
DR GeneID; 45425388; -.
DR KEGG; mbb:BCG_1471c; -.
DR HOGENOM; CLU_000960_2_5_11; -.
DR OMA; AGYWMTP; -.
DR Proteomes; UP000001472; 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 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Probable triacylglyceride transporter BCG_1471c"
FT /id="PRO_0000391004"
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
