LPQH_MYCTA
ID LPQH_MYCTA Reviewed; 159 AA.
AC A5U990;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Lipoprotein LpqH;
DE AltName: Full=19 kDa lipoprotein {ECO:0000303|PubMed:16547269};
DE AltName: Full=Putative transporter LpqH;
DE Flags: Precursor;
GN Name=lpqH; OrderedLocusNames=MRA_3801;
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.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=16547269; DOI=10.4049/jimmunol.176.7.4323;
RA Pennini M.E., Pai R.K., Schultz D.C., Boom W.H., Harding C.V.;
RT "Mycobacterium tuberculosis 19-kDa lipoprotein inhibits IFN-gamma-induced
RT chromatin remodeling of MHC2TA by TLR2 and MAPK signaling.";
RL J. Immunol. 176:4323-4330(2006).
RN [3]
RP FUNCTION IN INFECTION.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
RA Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
RA Golenbock D.T., Boom W.H., Harding C.V.;
RT "TLR2 and its co-receptors determine responses of macrophages and dendritic
RT cells to lipoproteins of Mycobacterium tuberculosis.";
RL Cell. Immunol. 258:29-37(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=26109643; DOI=10.4049/jimmunol.1402894;
RA Athman J.J., Wang Y., McDonald D.J., Boom W.H., Harding C.V., Wearsch P.A.;
RT "Bacterial membrane vesicles mediate the release of Mycobacterium
RT tuberculosis lipoglycans and lipoproteins from infected macrophages.";
RL J. Immunol. 195:1044-1053(2015).
RN [5]
RP REVIEW.
RX PubMed=20234378; DOI=10.1038/nrmicro2321;
RA Harding C.V., Boom W.H.;
RT "Regulation of antigen presentation by Mycobacterium tuberculosis: a role
RT for Toll-like receptors.";
RL Nat. Rev. Microbiol. 8:296-307(2010).
CC -!- FUNCTION: Might be involved in ligand transport (By similarity). A host
CC TLR2 agonist (toll-like receptor), shown experimentally for human and
CC mouse (PubMed:16547269, PubMed:19362712). Acts in host macrophages to
CC modify the expression of different subsets of interferon-gamma-induced
CC (IFN-g) genes, possibly by chromatin remodeling (PubMed:19362712).
CC Represses IFN-g induction of mouse macrophage MHC class II
CC transactivator (Ciita), greatly enhances IFN-g induction of mouse
CC macrophage inducible nitric oxide synthase (iNOS, Nos2)
CC (PubMed:19362712). At least for Ciita repression, acts via mouse TLR2
CC and MAPK to inhibit IFN-g-induced enrichment of acetylated histones H3
CC and H4 at the host Ciita but not at Nos2 loci (PubMed:19362712). Host
CC Ciita regulates the expression of MHC-II and other genes involved in Ag
CC processing and presentation, thus its repression contributes to immune
CC envasion by M.tuberculosis (PubMed:19362712). Requires both host TLR1
CC and TLR2 as coreceptors to elicit host response in mouse, although TLR6
CC may play a redundant role, and a partial requirement for CD14 as an
CC accessory receptor (PubMed:19362712). {ECO:0000250|UniProtKB:P9WK61,
CC ECO:0000269|PubMed:16547269, ECO:0000269|PubMed:19362712}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC Extracellular vesicle, bacterial extracellular vesicle
CC {ECO:0000269|PubMed:26109643}. Note=Found in bacterial extracytoplasmic
CC vesicles both in culture supernatant and isolated from infected mouse
CC macrophages: there is almost no co-localization of mouse and
CC M.tuberculosis markers in the vesicles, suggesting they do not mix
CC (PubMed:26109643). {ECO:0000269|PubMed:26109643}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
CC cavity. {ECO:0000250|UniProtKB:P9WK61}.
CC -!- PTM: Modified by Lgt on Cys-22 with an S-linked diacylglycerol with a
CC mixture of C16, C18 and C19 fatty acids, signal peptide is removed by
CC LspA, modifed by Lnt with an amide-linked mixture of C16 and C19 fatty
CC acids. {ECO:0000250|UniProtKB:P9WK61}.
CC -!- SIMILARITY: Belongs to the mycobacterial 19 kDa antigen family.
CC {ECO:0000305}.
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DR EMBL; CP000611; ABQ75590.1; -; Genomic_DNA.
DR RefSeq; WP_003420544.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U990; -.
DR SMR; A5U990; -.
DR STRING; 419947.MRA_3801; -.
DR EnsemblBacteria; ABQ75590; ABQ75590; MRA_3801.
DR GeneID; 45427763; -.
DR KEGG; mra:MRA_3801; -.
DR eggNOG; ENOG502ZGGY; Bacteria.
DR HOGENOM; CLU_117599_0_0_11; -.
DR OMA; CSDMGGN; -.
DR OrthoDB; 1980906at2; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR008691; LpqH.
DR Pfam; PF05481; Myco_19_kDa; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Signal; Transport;
KW Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..159
FT /note="Lipoprotein LpqH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000434897"
FT REGION 24..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 159 AA; 15147 MW; CB1A5090E14867BB CRC64;
MKRGLTVAVA GAAILVAGLS GCSSNKSTTG SGETTTAAGT TASPGAASGP KVVIDGKDQN
VTGSVVCTTA AGNVNIAIGG AATGIAAVLT DGNPPEVKSV GLGNVNGVTL GYTSGTGQGN
ASATKDGSHY KITGTATGVD MANPMSPVNK SFEIEVTCS
