Function

Probably helps membrane protein Rv1410c (P55) transport triacylglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation (PubMed:26751071). Binds TAG and transfers it between lipid bilayers, probably to the outer membrane in vivo (PubMed:26751071). Binds di- and triacylated phosphatidyl-myo-inositol mannosides (PIMs), and glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM), facilitating their recognition by TLR2 (PubMed:20694006, PubMed:25356793). Binds LM > PIM6 > ManLAM > PI-LAM > PIM2 (mannose-capped LAM and phospho-myo-inositol-capped LAM, E.coli expressed without acyl-groups); deacylated LM and LAM also bind to this protein via their mannose moieties, showing LprG has at least 2 different ways to bind glycolipids (PubMed:25356793). Binds triacylglycerides (TAG) in the same cavity, is able to transfer TAG between lipid bilayers (PubMed:26751071). Overexpression of LprG and Rv1410c leads to increased levels of TAG in the culture medium (PubMed:26751071). Required for Rv1410c-mediated export of drugs (PubMed:18156250, PubMed:21762531). Required, probably with Rv1410c, for normal surface localization of LAM (PubMed:25232742). {ECO:0000269|PubMed:18156250, ECO:0000269|PubMed:20694006, ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:25232742, ECO:0000269|PubMed:25356793, ECO:0000269|PubMed:26751071}.; FUNCTION: A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse (PubMed:19362712). Inhibits primary human macrophage MHC-II Ag processing via TLR2 (PubMed:15294983). Both lipidated and nonlipidated protein act as TLR2 agonists in antigen-presenting cells, although lipidated protein is more efficient (PubMed:20694006). In resting human CD4+ T-cells lipidated but not nonlipidated protein is a costimulatory ligand (with anti-CD3 and anti-CD28) for T-cell proliferation and IFN-gamma and IL-2 production, leading to increased expression of early T-cell activation markers, TLR2 and NFKB3 phosphorylation (PubMed:21078852). Human CD4+ T-cells use TLR1/TLR2 heterodimers to respond to this and probably other mycobacterial lipoproteins (PubMed:21078852). Able to stimulate proliferation of CD4+ T-cells derived from a human leprosy patient following protein processing/presentation by MHC class II molecules in peripheral blood mononuclear cells (PubMed:18424702). Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse, although TLR6 may play a redundant role, has a partial requirement for CD14 as an accessory receptor (PubMed:19362712). {ECO:0000269|PubMed:15294983, ECO:0000269|PubMed:18424702, ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:20694006, ECO:0000269|PubMed:21078852}.

Family

LppX/LprAFG lipoprotein family

GO

• lipid transport GO:0006869 biological_process
• phosphatidylinositol binding GO:0035091 molecular_function
• plasma membrane GO:0005886 cellular_component
• cell wall GO:0005618 cellular_component
• bacterial extracellular vesicle GO:0097691 cellular_component
• glycolipid binding GO:0051861 molecular_function
• pathogenesis GO:0009405 biological_process
• response to antibiotic GO:0046677 biological_process
• cell surface GO:0009986 cellular_component

InterPro

• IPR029046
• IPR009830

UniProt

P9WK45

GenBank

Rv1411c

EnsemblBacteria

Rv1411c

Mycobrowser

Rv1411c

Rv1411c doesn't seem to be a targeted by any drug.

• 

  Tuberculosis mtu05152

  mtu05152

  Human Diseases; Infectious disease: bacterial