LPRG_MYCBO
ID LPRG_MYCBO Reviewed; 236 AA.
AC P0A5I9; A0A1R3XY92; O32852; P71679; X2BHT9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Lipoarabinomannan carrier protein LprG;
DE AltName: Full=27 kDa lipoprotein {ECO:0000303|PubMed:9387238};
DE AltName: Full=Antigen P27 {ECO:0000303|PubMed:9387238};
DE AltName: Full=Lipoprotein LprG;
DE AltName: Full=Triacylglyceride transfer protein LprG;
DE Flags: Precursor;
GN Name=lprG; Synonyms=lpp-27 {ECO:0000303|PubMed:9387238};
GN OrderedLocusNames=BQ2027_MB1446C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=9598;
RX PubMed=9387238; DOI=10.1099/00221287-143-11-3599;
RA Bigi F., Espitia C., Alito A.E., Zumarraga M., Romano M.I., Cravero S.A.,
RA Cataldi A.;
RT "A novel 27 kDa lipoprotein antigen from Mycobacterium bovis.";
RL Microbiology 143:3599-3605(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Probably helps membrane protein Mb1445c (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 Mb1445c. Required, probably with Mb1445c, for normal
CC surface localization of LAM. {ECO:0000250|UniProtKB:P9WK45}.
CC -!- FUNCTION: Constitutes a host TLR2 agonist (toll-like receptor).
CC {ECO:0000250|UniProtKB:P9WK45}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:9387238, ECO:0000305}; Lipid-
CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Secreted, cell wall
CC {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). {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; AJ000500; CAA04135.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU00049.1; -; Genomic_DNA.
DR RefSeq; NP_855098.1; NC_002945.3.
DR RefSeq; WP_003407315.1; NC_002945.4.
DR AlphaFoldDB; P0A5I9; -.
DR SMR; P0A5I9; -.
DR EnsemblBacteria; SIU00049; SIU00049; BQ2027_MB1446C.
DR PATRIC; fig|233413.5.peg.1581; -.
DR OMA; TLTPNKW; -.
DR Proteomes; UP000001419; 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 3: Inferred from homology;
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_0000018144"
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
