LPRG_MYCTA
ID LPRG_MYCTA Reviewed; 236 AA.
AC A5U2B3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=MRA_1420;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=25356793; DOI=10.1371/journal.ppat.1004471;
RA Shukla S., Richardson E.T., Athman J.J., Shi L., Wearsch P.A., McDonald D.,
RA Banaei N., Boom W.H., Jackson M., Harding C.V.;
RT "Mycobacterium tuberculosis lipoprotein LprG binds lipoarabinomannan and
RT determines its cell envelope localization to control phagolysosomal
RT fusion.";
RL PLoS Pathog. 10:E1004471-E1004471(2014).
CC -!- FUNCTION: Probably helps membrane protein MRA_1419 (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 (PubMed:25356793). Probably facilitates recognition of glycolipids by
CC TLR2. Required for activity of drug efflux transporter MRA_1419.
CC Required, probably with MRA_1419, for normal surface localization of
CC LAM. {ECO:0000250|UniProtKB:P9WK45, ECO:0000305|PubMed:25356793}.
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 -!- DISRUPTION PHENOTYPE: Single deletion mutant (probably without
CC MRA_1419) has decreased surface-exposed glycolipid lipoarabinomannan
CC (LAM), although cellular LAM, LM and PIM content is normal
CC (PubMed:25356793). {ECO:0000269|PubMed:25356793}.
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|PubMed:25356793}.
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; CP000611; ABQ73163.1; -; Genomic_DNA.
DR RefSeq; WP_003407315.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U2B3; -.
DR SMR; A5U2B3; -.
DR STRING; 419947.MRA_1420; -.
DR EnsemblBacteria; ABQ73163; ABQ73163; MRA_1420.
DR KEGG; mra:MRA_1420; -.
DR eggNOG; ENOG50338Y0; Bacteria.
DR HOGENOM; CLU_074100_1_0_11; -.
DR OMA; TLTPNKW; -.
DR OrthoDB; 1542347at2; -.
DR Proteomes; UP000001988; 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 /id="PRO_0000434646"
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
