LPRG_MYCLE
ID LPRG_MYCLE Reviewed; 238 AA.
AC Q9CCP6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Lipoarabinomannan carrier protein LprG;
DE AltName: Full=27 kDa lipoprotein;
DE AltName: Full=Antigen P27;
DE AltName: Full=Lipoprotein LprG;
DE AltName: Full=Triacylglyceride transfer protein LprG;
DE Flags: Precursor;
GN Name=lprG; OrderedLocusNames=ML0557;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP FUNCTION IN INFECTION, AND GLYCOSYLATION.
RC STRAIN=TN;
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).
CC -!- FUNCTION: Probably helps membrane protein ML0556 (P55) transport
CC triacylglycerides (TAG) across the inner cell membrane into the
CC periplasm and probably ultimately to the outer membrane. TAG probably
CC regulates lipid metabolism and growth regulation. Binds di- and
CC triacylated phosphatidyl-myo-inositol mannosides (PIMs), and glycolipid
CC lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM),
CC facilitating their recognition by TLR2. Required for activity of drug
CC efflux transporter ML0556. Required, probably with ML0556, for normal
CC surface localization of LAM. {ECO:0000250|UniProtKB:P9WK45}.
CC -!- FUNCTION: Constitutes a host TLR2 agonist (toll-like receptor) able to
CC stimulate proliferation of CD4+ T-cells derived from a human leprosy
CC patient following protein processing/presentation by MHC class II
CC molecules in peripheral blood mononuclear cells.
CC {ECO:0000269|PubMed:18424702}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC Secreted, cell wall {ECO:0000250|UniProtKB:P9WK45}. Secreted
CC {ECO:0000250|UniProtKB:P9WK45}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a small hydrophobic
CC cavity able to hold a triacylated lipid or triacylglyceride.
CC {ECO:0000250|UniProtKB:P9WK45}.
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 (By
CC similarity). Probably glycosylated, which is required for T-cell
CC activation (PubMed:18424702). {ECO:0000250|UniProtKB:P9WK47,
CC ECO:0000269|PubMed:18424702}.
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.leprae, and are used as an energy source during
CC starvation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
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DR EMBL; AL583918; CAC30065.1; -; Genomic_DNA.
DR PIR; E86978; E86978.
DR RefSeq; NP_301471.1; NC_002677.1.
DR RefSeq; WP_010907795.1; NC_002677.1.
DR AlphaFoldDB; Q9CCP6; -.
DR SMR; Q9CCP6; -.
DR STRING; 272631.ML0557; -.
DR EnsemblBacteria; CAC30065; CAC30065; CAC30065.
DR KEGG; mle:ML0557; -.
DR PATRIC; fig|272631.5.peg.968; -.
DR Leproma; ML0557; -.
DR eggNOG; ENOG50338Y0; Bacteria.
DR HOGENOM; CLU_074100_1_0_11; -.
DR OMA; TLTPNKW; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; 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 Cell inner membrane; Cell membrane; Cell wall; Glycoprotein;
KW Lipid transport; Lipid-binding; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000305"
FT CHAIN 27..238
FT /note="Lipoarabinomannan carrier protein LprG"
FT /id="PRO_0000018145"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 24874 MW; F63E3725DCC7AE84 CRC64;
MQAPKHHRRL FAVLATLNTA TAVIAGCSSG SNLSSGPLPD ATTWVKQATD ITKNVTSAHL
VLSVNGKITG LPVKTLTGDL TTHPNTVASG NATITLDGAD LNANFVVVDG ELYATLTPSK
WSDFGKASDI YDVASILNPD AGLANVLANF TGAKTEGRDS INGQSAVRIS GNVSADAVNK
IAPPFNATQP MPATVWIQET GDHQLAQIRI DNKSSGNSVQ MTLSNWDEPV QVTKPQVS
