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Probable triacylglyceride transporter Rv1410c (MFS-type drug efflux transporter P55)

 MFS55_MYCTU             Reviewed;         518 AA.
P9WJY3; L0T9B4; P71678; Q7D8H0;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 24.
RecName: Full=Probable triacylglyceride transporter Rv1410c {ECO:0000303|PubMed:26751071};
AltName: Full=MFS-type drug efflux transporter P55;
OrderedLocusNames=Rv1410c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
DISRUPTION PHENOTYPE, AND VIRULENCE.
STRAIN=H37Rv;
PubMed=14998516; DOI=10.1016/j.micinf.2003.10.010;
Bigi F., Gioffre A., Klepp L., Santangelo M.P., Alito A., Caimi K.,
Meikle V., Zumarraga M., Taboga O., Romano M.I., Cataldi A.;
"The knockout of the lprG-Rv1410 operon produces strong attenuation of
Mycobacterium tuberculosis.";
Microbes Infect. 6:182-187(2004).
[3]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF ASP-22.
STRAIN=H37Rv;
PubMed=18156250; DOI=10.1128/JB.01046-07;
Farrow M.F., Rubin E.J.;
"Function of a mycobacterial major facilitator superfamily pump
requires a membrane-associated lipoprotein.";
J. Bacteriol. 190:1783-1791(2008).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=21762531; DOI=10.1186/1471-2334-11-195;
Bianco M.V., Blanco F.C., Imperiale B., Forrellad M.A., Rocha R.V.,
Klepp L.I., Cataldi A.A., Morcillo N., Bigi F.;
"Role of P27 -P55 operon from Mycobacterium tuberculosis in the
resistance to toxic compounds.";
BMC Infect. Dis. 11:195-195(2011).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=25232742; DOI=10.1371/journal.ppat.1004376;
Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
"LprG-mediated surface expression of lipoarabinomannan is essential
for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 10:E1004376-E1004376(2014).
[7]
ERRATUM.
PubMed=26650245; DOI=10.1371/journal.ppat.1005336;
Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
"Correction: LprG-mediated surface expression of lipoarabinomannan is
essential for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 11:E1005336-E1005336(2015).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25356793; DOI=10.1371/journal.ppat.1004471;
Shukla S., Richardson E.T., Athman J.J., Shi L., Wearsch P.A.,
McDonald D., Banaei N., Boom W.H., Jackson M., Harding C.V.;
"Mycobacterium tuberculosis lipoprotein LprG binds lipoarabinomannan
and determines its cell envelope localization to control
phagolysosomal fusion.";
PLoS Pathog. 10:E1004471-E1004471(2014).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=26751071; DOI=10.1371/journal.ppat.1005351;
Martinot A.J., Farrow M., Bai L., Layre E., Cheng T.Y., Tsai J.H.,
Iqbal J., Annand J.W., Sullivan Z.A., Hussain M.M., Sacchettini J.,
Moody D.B., Seeliger J.C., Rubin E.J.;
"Mycobacterial metabolic syndrome: LprG and Rv1410 regulate
triacylglyceride levels, growth rate and virulence in Mycobacterium
tuberculosis.";
PLoS Pathog. 12:E1005351-E1005351(2016).
-!- FUNCTION: In association with lipoprotein LprG probably transports
triacylglycerides (TAG) across the inner cell membrane into the
periplasm; TAG probably regulates lipid metabolism and growth
regulation (PubMed:26751071). Confers resistance to ethidium
bromide, possibly acting as an efflux pump, requires LprG
lipoprotein for normal function (PubMed:18156250). With LprG
maintains cell wall permeability (PubMed:21762531). Probably
required with LprG for normal surface localization of LAM
(PubMed:25232742, PubMed:25356793). Overexpression of LprG and
Rv1410c leads to increased levels of TAG in the culture medium
(PubMed:26751071). {ECO:0000269|PubMed:18156250,
ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:26751071,
ECO:0000305|PubMed:25232742, ECO:0000305|PubMed:25356793}.
-!- ENZYME REGULATION: Inhibited by reserpine (PubMed:18156250).
{ECO:0000269|PubMed:18156250}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:26751071}; Multi-pass membrane protein
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Disruption of only this gene, or of the
lrpG-Rv1410c operon leads to increased levels of many
triacylglyceride alkylforms; up to 100-fold increase depending on
the exact form (PubMed:26751071). Cells grow more slowly on lipid
carbon sources, conditions thought to mimic infection, and grow
more slowly in infected mice (PubMed:26751071). Disruption of the
preceeding gene lprG leads to loss of expression of Rv1410c due to
polar effects; in infected BALB/c mice 1.5 and 2.5 log decrease in
bacterial load 15 and 35 days after infection (PubMed:14998516).
The single lprG mutant increases sensitivity to malachite green,
sodium dodecyl sulfate (SDS), isoniazid, ethambutal and ethidium
bromide, alters the permeability of the cell wall; both genes are
required to fully restore the phenotypes (PubMed:21762531). Single
lprG deletion mutant (probably without Rv1410c) has decreased
surface-exposed glycolipid lipoarabinomannan (LAM), although
cellular LAM content is normal (PubMed:25232742, PubMed:25356793).
It also forms smaller colonies on agar (PubMed:25232742). Loss of
surface LAM has several consequences; bacteria enter mouse
macrophages with reduced efficiency and block mouse macrophage
phagosome-lysosome fusion less efficiently than wild-type
(PubMed:25232742). Reduced efficiency of mouse macrophage
phagosome-lysosome fusion was seen in another study
(PubMed:25356793). C57BL/6 mice infected with mutant bacteria have
10-fold less bacterial burden after 10 days and about 2700-fold
less burden after 70 days; attenuation of mutant is not rescued in
macrophages or mice impaired for reactive oxygen or nitrogen
generation (disruption of Ncf1 or iNOS) (PubMed:25232742,
PubMed:26751071). {ECO:0000269|PubMed:14998516,
ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:26751071,
ECO:0000305|PubMed:25232742, ECO:0000305|PubMed:25356793}.
-!- MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome
fusion and is one way in which M.tuberculosis evades the host
immune system. {ECO:0000305|PubMed:25232742,
ECO:0000305|PubMed:25356793}.
-!- MISCELLANEOUS: Triacylglycerides accumulate in lipid droplets in
the cytoplasm of M.tuberculosis stationary phase and dormant
bacteria, and are used as an energy source during starvation
(PubMed:26751071). {ECO:0000305|PubMed:26751071}.
-!- SIMILARITY: Belongs to the major facilitator superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL123456; CCP44169.1; -; Genomic_DNA.
PIR; G70901; G70901.
RefSeq; NP_215926.1; NC_000962.3.
RefSeq; WP_003407310.1; NZ_KK339370.1.
ProteinModelPortal; P9WJY3; -.
STRING; 83332.Rv1410c; -.
PaxDb; P9WJY3; -.
EnsemblBacteria; CCP44169; CCP44169; Rv1410c.
GeneID; 886709; -.
KEGG; mtu:Rv1410c; -.
KEGG; mtv:RVBD_1410c; -.
PATRIC; fig|83332.111.peg.1569; -.
TubercuList; Rv1410c; -.
eggNOG; ENOG4107UWP; Bacteria.
eggNOG; ENOG410ZXEF; LUCA.
OMA; AGYWMTP; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MTBBASE.
GO; GO:0008144; F:drug binding; IDA:MTBBASE.
GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0055085; P:transmembrane transport; IDA:MTBBASE.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 3.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Antibiotic resistance; Cell inner membrane; Cell membrane;
Complete proteome; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Virulence.
CHAIN 1 518 Probable triacylglyceride transporter
Rv1410c.
/FTId=PRO_0000391006.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TRANSMEM 76 96 Helical. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TRANSMEM 144 164 Helical. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TRANSMEM 201 221 Helical. {ECO:0000255}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
TRANSMEM 337 357 Helical. {ECO:0000255}.
TRANSMEM 379 401 Helical. {ECO:0000255}.
TRANSMEM 408 428 Helical. {ECO:0000255}.
TRANSMEM 475 495 Helical. {ECO:0000255}.
MUTAGEN 22 22 D->A: Susceptible to ethidium bromide,
tested in M.smegmatis.
{ECO:0000269|PubMed:18156250}.
MUTAGEN 22 22 D->E: Decreases resistance to ethidium
bromide, tested in M.smegmatis.
{ECO:0000269|PubMed:18156250}.
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


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