LPRG_MYCTU
ID LPRG_MYCTU Reviewed; 236 AA.
AC P9WK45; L0T868; O32852; P0A5I8; P71679;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Lipoarabinomannan carrier protein LprG {ECO:0000305|PubMed:25232742, ECO:0000305|PubMed:25356793};
DE AltName: Full=27 kDa lipoprotein;
DE AltName: Full=Antigen P27 {ECO:0000303|PubMed:14998516};
DE AltName: Full=Lipoprotein LprG;
DE AltName: Full=Triacylated glycolipid carrier LprG {ECO:0000303|PubMed:20694006};
DE AltName: Full=Triacylglyceride transfer protein LprG {ECO:0000303|PubMed:26751071};
DE Flags: Precursor;
GN Name=lprG; Synonyms=lpp-27; OrderedLocusNames=Rv1411c;
GN ORFNames=MTCY21B4.28c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE, AND VIRULENCE.
RC STRAIN=H37Rv;
RX PubMed=14998516; DOI=10.1016/j.micinf.2003.10.010;
RA Bigi F., Gioffre A., Klepp L., Santangelo M.P., Alito A., Caimi K.,
RA Meikle V., Zumarraga M., Taboga O., Romano M.I., Cataldi A.;
RT "The knockout of the lprG-Rv1410 operon produces strong attenuation of
RT Mycobacterium tuberculosis.";
RL Microbes Infect. 6:182-187(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15294983; DOI=10.4049/jimmunol.173.4.2660;
RA Gehring A.J., Dobos K.M., Belisle J.T., Harding C.V., Boom W.H.;
RT "Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that
RT inhibits human macrophage class II MHC antigen processing.";
RL J. Immunol. 173:2660-2668(2004).
RN [4]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=18156250; DOI=10.1128/jb.01046-07;
RA Farrow M.F., Rubin E.J.;
RT "Function of a mycobacterial major facilitator superfamily pump requires a
RT membrane-associated lipoprotein.";
RL J. Bacteriol. 190:1783-1791(2008).
RN [5]
RP FUNCTION IN INFECTION, AND GLYCOSYLATION.
RX PubMed=18424702; DOI=10.4049/jimmunol.180.9.5833;
RA Sieling P.A., Hill P.J., Dobos K.M., Brookman K., Kuhlman A.M., Fabri M.,
RA Krutzik S.R., Rea T.H., Heaslip D.G., Belisle J.T., Modlin R.L.;
RT "Conserved mycobacterial lipoglycoproteins activate TLR2 but also require
RT glycosylation for MHC class II-restricted T cell activation.";
RL J. Immunol. 180:5833-5842(2008).
RN [6]
RP FUNCTION IN INFECTION.
RC STRAIN=H37Rv;
RX PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
RA Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
RA Golenbock D.T., Boom W.H., Harding C.V.;
RT "TLR2 and its co-receptors determine responses of macrophages and dendritic
RT cells to lipoproteins of Mycobacterium tuberculosis.";
RL Cell. Immunol. 258:29-37(2009).
RN [7]
RP FUNCTION, AND GLYCOSYLATION.
RC STRAIN=ATCC 25177 / H37Ra, and H37Rv;
RX PubMed=21078852; DOI=10.1128/iai.00806-10;
RA Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
RA Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H., Rojas R.E.;
RT "Mycobacterium tuberculosis lipoproteins directly regulate human memory
RT CD4(+) T cell activation via Toll-like receptors 1 and 2.";
RL Infect. Immun. 79:663-673(2011).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=21364279; DOI=10.1172/jci44261;
RA Prados-Rosales R., Baena A., Martinez L.R., Luque-Garcia J., Kalscheuer R.,
RA Veeraraghavan U., Camara C., Nosanchuk J.D., Besra G.S., Chen B.,
RA Jimenez J., Glatman-Freedman A., Jacobs W.R. Jr., Porcelli S.A.,
RA Casadevall A.;
RT "Mycobacteria release active membrane vesicles that modulate immune
RT responses in a TLR2-dependent manner in mice.";
RL J. Clin. Invest. 121:1471-1483(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=21762531; DOI=10.1186/1471-2334-11-195;
RA Bianco M.V., Blanco F.C., Imperiale B., Forrellad M.A., Rocha R.V.,
RA Klepp L.I., Cataldi A.A., Morcillo N., Bigi F.;
RT "Role of P27 -P55 operon from Mycobacterium tuberculosis in the resistance
RT to toxic compounds.";
RL BMC Infect. Dis. 11:195-195(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [11]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25041568; DOI=10.1111/cbdd.12365;
RA Ocampo M., Curtidor H., Vanegas M., Patarroyo M.A., Patarroyo M.E.;
RT "Specific interaction between Mycobacterium tuberculosis lipoprotein-
RT derived peptides and target cells inhibits mycobacterial entry in vitro.";
RL Chem. Biol. Drug Des. 84:626-641(2014).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=25232742; DOI=10.1371/journal.ppat.1004376;
RA Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
RA Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
RT "LprG-mediated surface expression of lipoarabinomannan is essential for
RT virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 10:E1004376-E1004376(2014).
RN [13]
RP ERRATUM OF PUBMED:25232742.
RX PubMed=26650245; DOI=10.1371/journal.ppat.1005336;
RA Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
RA Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
RT "Correction: LprG-mediated surface expression of lipoarabinomannan is
RT essential for virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 11:E1005336-E1005336(2015).
RN [14]
RP FUNCTION, LIPID-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-91.
RC STRAIN=H37Rv;
RX PubMed=25356793; DOI=10.1371/journal.ppat.1004471;
RA Shukla S., Richardson E.T., Athman J.J., Shi L., Wearsch P.A., McDonald D.,
RA Banaei N., Boom W.H., Jackson M., Harding C.V.;
RT "Mycobacterium tuberculosis lipoprotein LprG binds lipoarabinomannan and
RT determines its cell envelope localization to control phagolysosomal
RT fusion.";
RL PLoS Pathog. 10:E1004471-E1004471(2014).
RN [15]
RP REVIEW.
RX PubMed=20234378; DOI=10.1038/nrmicro2321;
RA Harding C.V., Boom W.H.;
RT "Regulation of antigen presentation by Mycobacterium tuberculosis: a role
RT for Toll-like receptors.";
RL Nat. Rev. Microbiol. 8:296-307(2010).
RN [16] {ECO:0007744|PDB:3MH8, ECO:0007744|PDB:3MH9, ECO:0007744|PDB:3MHA}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 28-236, FUNCTION, DOMAIN,
RP LIPID-BINDING, PALMITOYLATION AT CYS-27, DIACYLGLYCEROL AT CYS-27, AND
RP MUTAGENESIS OF VAL-91.
RC STRAIN=H37Rv;
RX PubMed=20694006; DOI=10.1038/nsmb.1869;
RA Drage M.G., Tsai H.C., Pecora N.D., Cheng T.Y., Arida A.R., Shukla S.,
RA Rojas R.E., Seshadri C., Moody D.B., Boom W.H., Sacchettini J.C.,
RA Harding C.V.;
RT "Mycobacterium tuberculosis lipoprotein LprG (Rv1411c) binds triacylated
RT glycolipid agonists of Toll-like receptor 2.";
RL Nat. Struct. Mol. Biol. 17:1088-1095(2010).
RN [17] {ECO:0007744|PDB:4ZRA}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 36-231 IN COMPLEX WITH
RP TRIACYLGLYCERIDE, FUNCTION, DOMAIN, TRIACYLGLYCERIDE-BINDING, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF VAL-91.
RC STRAIN=H37Rv;
RX PubMed=26751071; DOI=10.1371/journal.ppat.1005351;
RA Martinot A.J., Farrow M., Bai L., Layre E., Cheng T.Y., Tsai J.H.,
RA Iqbal J., Annand J.W., Sullivan Z.A., Hussain M.M., Sacchettini J.,
RA Moody D.B., Seeliger J.C., Rubin E.J.;
RT "Mycobacterial metabolic syndrome: LprG and Rv1410 regulate
RT triacylglyceride levels, growth rate and virulence in Mycobacterium
RT tuberculosis.";
RL PLoS Pathog. 12:E1005351-E1005351(2016).
CC -!- FUNCTION: Probably helps membrane protein Rv1410c (P55) transport
CC triacylglycerides (TAG) across the inner cell membrane into the
CC periplasm; TAG probably regulates lipid metabolism and growth
CC regulation (PubMed:26751071). Binds TAG and transfers it between lipid
CC bilayers, probably to the outer membrane in vivo (PubMed:26751071).
CC Binds di- and triacylated phosphatidyl-myo-inositol mannosides (PIMs),
CC and glycolipid lipoglycan modulins lipoarabinomannan (LAM) and
CC lipomannan (LM), facilitating their recognition by TLR2
CC (PubMed:20694006, PubMed:25356793). Binds LM > PIM6 > ManLAM > PI-LAM >
CC PIM2 (mannose-capped LAM and phospho-myo-inositol-capped LAM, E.coli
CC expressed without acyl-groups); deacylated LM and LAM also bind to this
CC protein via their mannose moieties, showing LprG has at least 2
CC different ways to bind glycolipids (PubMed:25356793). Binds
CC triacylglycerides (TAG) in the same cavity, is able to transfer TAG
CC between lipid bilayers (PubMed:26751071). Overexpression of LprG and
CC Rv1410c leads to increased levels of TAG in the culture medium
CC (PubMed:26751071). Required for Rv1410c-mediated export of drugs
CC (PubMed:18156250, PubMed:21762531). Required, probably with Rv1410c,
CC for normal surface localization of LAM (PubMed:25232742).
CC {ECO:0000269|PubMed:18156250, ECO:0000269|PubMed:20694006,
CC ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:25232742,
CC ECO:0000269|PubMed:25356793, ECO:0000269|PubMed:26751071}.
CC -!- FUNCTION: A host TLR2 agonist (toll-like receptor), shown
CC experimentally for human and mouse (PubMed:19362712). Inhibits primary
CC human macrophage MHC-II Ag processing via TLR2 (PubMed:15294983). Both
CC lipidated and nonlipidated protein act as TLR2 agonists in antigen-
CC presenting cells, although lipidated protein is more efficient
CC (PubMed:20694006). In resting human CD4+ T-cells lipidated but not
CC nonlipidated protein is a costimulatory ligand (with anti-CD3 and anti-
CC CD28) for T-cell proliferation and IFN-gamma and IL-2 production,
CC leading to increased expression of early T-cell activation markers,
CC TLR2 and NFKB3 phosphorylation (PubMed:21078852). Human CD4+ T-cells
CC use TLR1/TLR2 heterodimers to respond to this and probably other
CC mycobacterial lipoproteins (PubMed:21078852). Able to stimulate
CC proliferation of CD4+ T-cells derived from a human leprosy patient
CC following protein processing/presentation by MHC class II molecules in
CC peripheral blood mononuclear cells (PubMed:18424702). Requires both
CC host TLR1 and TLR2 as coreceptors to elicit host response in mouse,
CC although TLR6 may play a redundant role, has a partial requirement for
CC CD14 as an accessory receptor (PubMed:19362712).
CC {ECO:0000269|PubMed:15294983, ECO:0000269|PubMed:18424702,
CC ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:20694006,
CC ECO:0000269|PubMed:21078852}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:21762531, ECO:0000305}; Lipid-
CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Secreted, cell wall
CC {ECO:0000269|PubMed:21762531}. Secreted {ECO:0000269|PubMed:21762531}.
CC Cell surface {ECO:0000269|PubMed:25041568}. Note=Present in
CC extracytoplasmic vesicles (PubMed:21364279). Immunoelectron microscopy
CC indicates this protein is close to the cell surface (PubMed:25041568).
CC {ECO:0000269|PubMed:21364279, ECO:0000269|PubMed:25041568}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a small hydrophobic
CC cavity (1500 Angstroms (3)) which holds a triacylated PIM in 1 crystal
CC structure; the 3 acyl chains are within the cavity while the sugar
CC moieties bind to the protein surface (PubMed:20694006). In the
CC structure bound to triacylglycerides (TAG) 2 of the 3 acyl chains are
CC buried in the cavity, the third is solvent exposed (PubMed:26751071). A
CC flexible lid region may move to accommodate different TAG molecules
CC (PubMed:26751071). Fragments of the mature protein (residues 81-100,
CC 141-160 and 218-236) prevent uptake of M.tuberculosis by a human
CC macrophage-like cell line; lesser effects are seen on bacterial uptake
CC by a human lung epithelial cell line (PubMed:25041568).
CC {ECO:0000269|PubMed:20694006, ECO:0000269|PubMed:25041568,
CC ECO:0000269|PubMed:26751071}.
CC -!- PTM: Modified by Lgt on Cys-27 with an S-linked diacylglyceral, signal
CC peptide is removed by LspA, Cys-27 is further modifed with a fatty acid
CC on its amino group by Lnt yielding a triacylated protein (Probable).
CC Probably glycosylated, which is required for T-cell activation
CC (PubMed:18424702). {ECO:0000250|UniProtKB:P9WK47,
CC ECO:0000269|PubMed:18424702, ECO:0000305|PubMed:20694006}.
CC -!- DISRUPTION PHENOTYPE: A single deletion mutant leads to loss of
CC expression of efflux pump Rv1410c due to polar effects; in infected
CC BALB/c mice 1.5 and 2.5 log decrease in bacterial load 15 and 35 days
CC after infection (PubMed:14998516). The single mutant increases
CC sensitivity to malachite green, sodium dodecyl sulfate (SDS),
CC isoniazid, ethambutal and ethidium bromide, alters the permeability of
CC the cell wall; both genes of the operon are required to fully restore
CC the phenotypes (PubMed:21762531). Single deletion mutant (probably
CC without Rv1410c) has decreased surface-exposed glycolipid
CC lipoarabinomannan (LAM), although cellular LAM, LM and PIM content is
CC normal (PubMed:25232742, PubMed:25356793). Disruption of either Rv1410c
CC or the lrpG-Rv1410c operon leads to increased levels of many
CC triacylglyceride (TAG) alkylforms; up to 100-fold increase depending on
CC the exact TAG form (PubMed:26751071). It also forms smaller colonies on
CC agar (PubMed:25232742). Loss of surface LAM has several consequences;
CC bacteria enter mouse macrophages with reduced efficiency and block
CC mouse macrophage phagosome-lysosome fusion less efficiently than wild-
CC type (PubMed:25232742). Reduced efficiency of mouse macrophage
CC phagosome-lysosome fusion was seen in another study (PubMed:25356793).
CC C57BL/6 mice infected with mutant bacteria have 10-fold less bacterial
CC burden after 10 days and about 2700-fold less burden after 70 days;
CC attenuation of mutant is not rescued in macrophages impaired for
CC reactive oxygen or nitrogen generation (disruption of Ncf1 or iNOS)
CC (PubMed:25232742). {ECO:0000269|PubMed:14998516,
CC ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:25232742,
CC ECO:0000269|PubMed:25356793, ECO:0000269|PubMed:26751071}.
CC -!- MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome fusion
CC and is one way in which M.tuberculosis evades the host immune system.
CC {ECO:0000305|PubMed:25232742, ECO:0000305|PubMed:25356793}.
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 (PubMed:26751071).
CC {ECO:0000305|PubMed:26751071}.
CC -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44170.1; -; Genomic_DNA.
DR PIR; H70901; H70901.
DR RefSeq; NP_215927.1; NC_000962.3.
DR RefSeq; WP_003407315.1; NZ_NVQJ01000038.1.
DR PDB; 3MH8; X-ray; 2.00 A; A/B=36-231.
DR PDB; 3MH9; X-ray; 1.79 A; A/C=28-236.
DR PDB; 3MHA; X-ray; 1.85 A; A/B=36-231.
DR PDB; 4ZRA; X-ray; 1.83 A; A/C=36-231.
DR PDBsum; 3MH8; -.
DR PDBsum; 3MH9; -.
DR PDBsum; 3MHA; -.
DR PDBsum; 4ZRA; -.
DR AlphaFoldDB; P9WK45; -.
DR SMR; P9WK45; -.
DR STRING; 83332.Rv1411c; -.
DR PaxDb; P9WK45; -.
DR DNASU; 886700; -.
DR GeneID; 886700; -.
DR KEGG; mtu:Rv1411c; -.
DR TubercuList; Rv1411c; -.
DR eggNOG; ENOG50338Y0; Bacteria.
DR OMA; TLTPNKW; -.
DR PhylomeDB; P9WK45; -.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR PHI-base; PHI:5579; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0051861; F:glycolipid binding; IDA:MTBBASE.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd16334; LppX-like; 1.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR009830; LppX/LprAFG.
DR Pfam; PF07161; LppX_LprAFG; 1.
DR SUPFAM; SSF89392; SSF89392; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Cell wall; Glycoprotein; Lipid transport; Lipid-binding; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Secreted; Signal; Transport;
KW Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 27..236
FT /note="Lipoarabinomannan carrier protein LprG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000018146"
FT REGION 81..100
FT /note="Prevents bacterial uptake by a human macrophage-like
FT cell line"
FT /evidence="ECO:0000269|PubMed:25041568"
FT REGION 141..160
FT /note="Prevents bacterial uptake by a human macrophage-like
FT cell line"
FT /evidence="ECO:0000269|PubMed:25041568"
FT REGION 218..236
FT /note="Prevents bacterial uptake by a human macrophage-like
FT cell line"
FT /evidence="ECO:0000269|PubMed:25041568"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:20694006"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:20694006"
FT MUTAGEN 91
FT /note="V->W: Decreased TLR2 agonist activity, cannot
FT acquire lipid from mycobacterial extracts, cavity entrance
FT and size decrease. Binds PIM6, LM and ManLAM 10-100-fold
FT less well than wild-type, binds de-acylated LM and ManLAM
FT as well as wild-type. Decreased ability to transfer
FT triacylglyceride between lipid bilayers."
FT /evidence="ECO:0000269|PubMed:20694006,
FT ECO:0000269|PubMed:25356793, ECO:0000269|PubMed:26751071"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:3MH9"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3MH9"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3MH9"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3MH9"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3MH9"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:3MH9"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3MH9"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:3MH9"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:3MH9"
SQ SEQUENCE 236 AA; 24548 MW; 2591DAE6D2E2DC22 CRC64;
MRTPRRHCRR IAVLAAVSIA ATVVAGCSSG SKPSGGPLPD AKPLVEEATA QTKALKSAHM
VLTVNGKIPG LSLKTLSGDL TTNPTAATGN VKLTLGGSDI DADFVVFDGI LYATLTPNQW
SDFGPAADIY DPAQVLNPDT GLANVLANFA DAKAEGRDTI NGQNTIRISG KVSAQAVNQI
APPFNATQPV PATVWIQETG DHQLAQAQLD RGSGNSVQMT LSKWGEKVQV TKPPVS
