ID   LPRG_MYCTO              Reviewed;         236 AA.
AC   P9WK44; L0T868; O32852; P0A5I8; P71679;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
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; Synonyms=lpp-27; OrderedLocusNames=MT1455;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Probably helps membrane protein MT1454 (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 MT1454. Required, probably with MT1454, 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}; 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). {ECO:0000250|UniProtKB:P9WK47}.
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}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45720.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45720.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70901; H70901.
DR   RefSeq; WP_003407315.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK44; -.
DR   SMR; P9WK44; -.
DR   EnsemblBacteria; AAK45720; AAK45720; MT1455.
DR   KEGG; mtc:MT1455; -.
DR   PATRIC; fig|83331.31.peg.1563; -.
DR   HOGENOM; CLU_074100_1_0_11; -.
DR   Proteomes; UP000001020; 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:0000305"
FT   CHAIN           27..236
FT                   /note="Lipoarabinomannan carrier protein LprG"
FT                   /id="PRO_0000427718"
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   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