LPRG_MYCBP
ID LPRG_MYCBP Reviewed; 236 AA.
AC A0A0H3M3S8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 25.
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=BCG_1472c;
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, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN
RP CD209.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
RA Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R., Mitchell D.A.;
RT "Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.";
RL Protein Cell 1:859-870(2010).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=BCG / Pasteur 1173P2;
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).
CC -!- FUNCTION: Probably helps membrane protein BCG_1471c (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 BCG_1471c. Required, probably with BCG_1471c, for
CC normal surface localization of LAM. {ECO:0000250|UniProtKB:P9WK45}.
CC -!- FUNCTION: Constitutes a host TLR2 agonist (toll-like receptor) (By
CC similarity). In vitro binds to human CD209 (DC-SIGN) and CD209-like
CC antigen (CLEC4M) and may help mediate adherence to host cells
CC (PubMed:21203928). {ECO:0000250|UniProtKB:P9WK45,
CC ECO:0000269|PubMed:21203928}.
CC -!- SUBUNIT: In vitro able to bind to host (human) CD209, may also bind
CC CD209-like antigen (CLEC4M) (PubMed:21203928).
CC {ECO:0000269|PubMed:21203928}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WK45}.
CC Secreted {ECO:0000250|UniProtKB:P9WK45}. Note=Present in
CC extracytoplasmic vesicles (PubMed:21364279).
CC {ECO:0000269|PubMed:21364279}.
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). {ECO:0000250|UniProtKB:P9WK47}.
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 LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
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DR EMBL; AM408590; CAL71459.1; -; Genomic_DNA.
DR RefSeq; WP_003407315.1; NC_008769.1.
DR AlphaFoldDB; A0A0H3M3S8; -.
DR SMR; A0A0H3M3S8; -.
DR KEGG; mbb:BCG_1472c; -.
DR HOGENOM; CLU_074100_1_0_11; -.
DR OMA; TLTPNKW; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
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; Lipid transport;
KW Lipid-binding; Lipoprotein; Membrane; Palmitate; Secreted; Signal;
KW Transport.
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_0000434645"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
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
