LPQH_MYCTU
ID LPQH_MYCTU Reviewed; 159 AA.
AC P9WK61; L0TGP1; P0A5J0; P11572;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Lipoprotein LpqH;
DE AltName: Full=19 kDa lipoprotein antigen;
DE AltName: Full=Putative transporter LpqH {ECO:0000305|Ref.25};
DE AltName: Full=p19 {ECO:0000303|PubMed:12594264};
DE Flags: Precursor;
GN Name=lpqH; OrderedLocusNames=Rv3763; ORFNames=MTV025.111;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=2493628; DOI=10.1093/nar/17.3.1249;
RA Ashbridge K.R., Booth R.J., Watson J.D., Lathigra R.B.;
RT "Nucleotide sequence of the 19 kDa antigen gene from Mycobacterium
RT tuberculosis.";
RL Nucleic Acids Res. 17:1249-1249(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3132709; DOI=10.1073/pnas.85.12.4267;
RA Young D., Lathigra R., Hendrix R., Sweetser D., Young R.A.;
RT "Stress proteins are immune targets in leprosy and tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4267-4270(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-22.
RC STRAIN=H37Rv;
RX PubMed=1906192; DOI=10.1016/0923-2508(91)90097-t;
RA Young D.B., Garbe T.R.;
RT "Lipoprotein antigens of Mycobacterium tuberculosis.";
RL Res. Microbiol. 142:55-65(1991).
RN [5]
RP GLYCOSYLATION, EXPRESSION IN M.SMEGMATIS AND M.VACCAE, AND MUTAGENESIS OF
RP 34-THR--THR-36; 34-THR--THR-41 AND 40-THR-THR-41.
RX PubMed=8670858; DOI=10.1002/j.1460-2075.1996.tb00724.x;
RA Herrmann J.L., O'Gaora P., Gallagher A., Thole J.E., Young D.B.;
RT "Bacterial glycoproteins: a link between glycosylation and proteolytic
RT cleavage of a 19 kDa antigen from Mycobacterium tuberculosis.";
RL EMBO J. 15:3547-3554(1996).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=10426995; DOI=10.1126/science.285.5428.732;
RA Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
RA Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
RA Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
RT "Host defense mechanisms triggered by microbial lipoproteins through Toll-
RT like receptors.";
RL Science 285:732-736(1999).
RN [7]
RP SUBCELLULAR LOCATION DURING INFECTION, AND MUTAGENESIS OF CYS-22 AND
RP 34-THR--THR-41.
RC STRAIN=H37Rv;
RX PubMed=11123323; DOI=10.4049/jimmunol.166.1.447;
RA Neyrolles O., Gould K., Gares M.P., Brett S., Janssen R., O'Gaora P.,
RA Herrmann J.L., Prevost M.C., Perret E., Thole J.E., Young D.;
RT "Lipoprotein access to MHC class I presentation during infection of murine
RT macrophages with live mycobacteria.";
RL J. Immunol. 166:447-457(2001).
RN [8]
RP FUNCTION IN DENDRITIC CELL MATURATION.
RX PubMed=11160304; DOI=10.4049/jimmunol.166.4.2444;
RA Hertz C.J., Kiertscher S.M., Godowski P.J., Bouis D.A., Norgard M.V.,
RA Roth M.D., Modlin R.L.;
RT "Microbial lipopeptides stimulate dendritic cell maturation via Toll-like
RT receptor 2.";
RL J. Immunol. 166:2444-2450(2001).
RN [9]
RP FUNCTION.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=11441098; DOI=10.4049/jimmunol.167.2.910;
RA Noss E.H., Pai R.K., Sellati T.J., Radolf J.D., Belisle J., Golenbock D.T.,
RA Boom W.H., Harding C.V.;
RT "Toll-like receptor 2-dependent inhibition of macrophage class II MHC
RT expression and antigen processing by 19-kDa lipoprotein of Mycobacterium
RT tuberculosis.";
RL J. Immunol. 167:910-918(2001).
RN [10]
RP FUNCTION IN HOST APOPTOSIS.
RX PubMed=12594264; DOI=10.4049/jimmunol.170.5.2409;
RA Lopez M., Sly L.M., Luu Y., Young D., Cooper H., Reiner N.E.;
RT "The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis
RT through Toll-like receptor-2.";
RL J. Immunol. 170:2409-2416(2003).
RN [11]
RP FUNCTION IN HOST IFN-G SIGNALING, AND DOES NOT CAUSE HOST APOPTOSIS.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=12874328; DOI=10.1128/iai.71.8.4487-4497.2003;
RA Gehring A.J., Rojas R.E., Canaday D.H., Lakey D.L., Harding C.V.,
RA Boom W.H.;
RT "The Mycobacterium tuberculosis 19-kilodalton lipoprotein inhibits gamma
RT interferon-regulated HLA-DR and Fc gamma R1 on human macrophages through
RT Toll-like receptor 2.";
RL Infect. Immun. 71:4487-4497(2003).
RN [12]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND EXPRESSION IN M.SMEGMATIS.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=16098710; DOI=10.1016/j.micpath.2005.06.002;
RA Diaz-Silvestre H., Espinosa-Cueto P., Sanchez-Gonzalez A.,
RA Esparza-Ceron M.A., Pereira-Suarez A.L., Bernal-Fernandez G., Espitia C.,
RA Mancilla R.;
RT "The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin that
RT binds the mannose receptor of THP-1 monocytic cells and promotes
RT phagocytosis of mycobacteria.";
RL Microb. Pathog. 39:97-107(2005).
RN [13]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=16177361; DOI=10.1128/iai.73.10.6831-6837.2005;
RA Stewart G.R., Wilkinson K.A., Newton S.M., Sullivan S.M., Neyrolles O.,
RA Wain J.R., Patel J., Pool K.L., Young D.B., Wilkinson R.J.;
RT "Effect of deletion or overexpression of the 19-kilodalton lipoprotein
RT Rv3763 on the innate response to Mycobacterium tuberculosis.";
RL Infect. Immun. 73:6831-6837(2005).
RN [14]
RP FUNCTION.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=16622205; DOI=10.1128/iai.74.5.2686-2696.2006;
RA Jung S.B., Yang C.S., Lee J.S., Shin A.R., Jung S.S., Son J.W.,
RA Harding C.V., Kim H.J., Park J.K., Paik T.H., Song C.H., Jo E.K.;
RT "The mycobacterial 38-kilodalton glycolipoprotein antigen activates the
RT mitogen-activated protein kinase pathway and release of proinflammatory
RT cytokines through Toll-like receptors 2 and 4 in human monocytes.";
RL Infect. Immun. 74:2686-2696(2006).
RN [15]
RP DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=H37Rv;
RX PubMed=17804126; DOI=10.1016/j.vaccine.2007.07.042;
RA Henao-Tamayo M., Junqueira-Kipnis A.P., Ordway D., Gonzales-Juarrero M.,
RA Stewart G.R., Young D.B., Wilkinson R.J., Basaraba R.J., Orme I.M.;
RT "A mutant of Mycobacterium tuberculosis lacking the 19-kDa lipoprotein
RT Rv3763 is highly attenuated in vivo but retains potent vaccinogenic
RT properties.";
RL Vaccine 25:7153-7159(2007).
RN [16]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=21078852; DOI=10.1128/iai.00806-10;
RA Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
RA Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H., Rojas R.E.;
RT "Mycobacterium tuberculosis lipoproteins directly regulate human memory
RT CD4(+) T cell activation via Toll-like receptors 1 and 2.";
RL Infect. Immun. 79:663-673(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
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).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [19]
RP FUNCTION IN HOST APOPTOSIS.
RX PubMed=23316255; DOI=10.1155/2012/950503;
RA Sanchez A., Espinosa P., Garcia T., Mancilla R.;
RT "The 19 kDa Mycobacterium tuberculosis lipoprotein (LpqH) induces
RT macrophage apoptosis through extrinsic and intrinsic pathways: a role for
RT the mitochondrial apoptosis-inducing factor.";
RL Clin. Dev. Immunol. 2012:950503-950503(2012).
RN [20]
RP MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-22, PALMITOYLATION AT CYS-22,
RP LIPIDATION, POST-TRANSLATIONAL MODIFICATION, AND EXPRESSION IN M.BOVIS.
RC STRAIN=H37Rv;
RX PubMed=24093492; DOI=10.1186/1471-2180-13-223;
RA Bruelle J.K., Tschumi A., Sander P.;
RT "Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are
RT N-acylated by apolipoprotein N-acyltransferase BCG_2070c.";
RL BMC Microbiol. 13:223-223(2013).
RN [21]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25041568; DOI=10.1111/cbdd.12365;
RA Ocampo M., Curtidor H., Vanegas M., Patarroyo M.A., Patarroyo M.E.;
RT "Specific interaction between Mycobacterium tuberculosis lipoprotein-
RT derived peptides and target cells inhibits mycobacterial entry in vitro.";
RL Chem. Biol. Drug Des. 84:626-641(2014).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=H37Rv;
RX PubMed=25359607; DOI=10.1111/sji.12249;
RA Esparza M., Palomares B., Garcia T., Espinosa P., Zenteno E., Mancilla R.;
RT "PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an adhesin,
RT which binds the macrophage mannose receptor and promotes phagocytosis.";
RL Scand. J. Immunol. 81:46-55(2015).
RN [23]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25504154; DOI=10.3892/mmr.2014.3070;
RA Liu L., Liu J., Niu G., Xu Q., Chen Q.;
RT "Mycobacterium tuberculosis 19-kDa lipoprotein induces Toll-like receptor
RT 2-dependent peroxisome proliferator-activated receptor gamma expression and
RT promotes inflammatory responses in human macrophages.";
RL Mol. Med. Report. 11:2921-2926(2015).
RN [24]
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).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 48-159, PUTATIVE FUNCTION,
RP DOMAIN, AND DISULFIDE BOND.
RC STRAIN=H37Rv;
RA Arbing M.A., Chan S., Kuo E., Harris L.R., Zhou T.T., Eisenberg D.;
RT "Crystal structure of Mycobacterium tuberculosis LpqH (Rv3763).";
RL Submitted (APR-2015) to the PDB data bank.
CC -!- FUNCTION: Based on its structure might be involved in ligand transport
CC (Ref.25) (By similarity). {ECO:0000250|UniProtKB:P65307,
CC ECO:0000305|Ref.25}.
CC -!- FUNCTION: A host TLR2 agonist (PubMed:10426995, PubMed:11441098,
CC PubMed:12874328). Plays a complicated role in bacterial interactions
CC with the host immune system; some effects favor the host (induces
CC interleukin 1-beta and IL-12 p40 (IL12B), both increase the host's
CC immune response) while others favor the bacteria (increases growth in
CC monocyte-derived macrophages and decreases host MHC class II (MHC-II)
CC expression and antigen processing) (PubMed:16177361). Induces host
CC (human and mouse) IL-12 p40 (IL12B, a pro-inflammatory cytokine)
CC release by monocyte cell lines via TLR2 and CD14 (PubMed:10426995).
CC Induces host (human) monocytes to produce TNF-alpha, IL-6 and IL-12
CC p40; LpqH is a more potent inducer than PstS1 (PubMed:16622205).
CC Inhibits MHC-II expression and antigen processing in host (mouse)
CC macrophages via TLR2 (independently of TLR4) probably via the lipid
CC modification (PubMed:11441098). Stimulates host (human) dendritic cell
CC maturation to become MHC-II-positive antigen presenting cells via TLR2,
CC which depends on lipidation; nonlipidated protein does not stimulate
CC maturation (PubMed:11160304). Inhibits host (human and mouse) IFN-gamma
CC signaling in macrophages via TLR2; decreases IFN-gamma stimulated MHC-
CC II antigen processing as well as decreasing IFN-gamma-mediated up-
CC regulation of immunoglobulin gamma Fc receptor (FCGR1A), enabling the
CC bacteria to evade the immune system (PubMed:12874328). In resting human
CC CD4+ T-cells lipidated (but probably not nonlipidated protein) is a
CC costimulatory ligand (with anti-CD3 and anti-CD28) for T-cell
CC proliferation and IFN-gamma and IL-2 production (PubMed:21078852).
CC Human CD4+ T-cells probably use TLR1/TLR2 heterodimers to respond to
CC mycobacterial lipoproteins (PubMed:21078852). Acting via TLR2 enhances
CC expression of host peroxisome proliferator-activated receptor gamma
CC (PPARG), a regulator of inflammation and immunoregulation, and
CC increases p38 MAPK phosphorylation, IL-6 and TNF-alpha expression
CC (PubMed:25504154). Native or nonlipidated recombinant protein missing
CC the first 4 residues have been shown to induce apoptosis in the human
CC macrophage cell line THP-1 and human monocyte-derived macrophages in a
CC TLR2, caspase-3 and caspase-8-dependent manner (PubMed:12594264).
CC Protein overexpressed in M.smegmatis (lipidated and probably
CC glycosylated) induces apoptosis in human macrophages via TLR2 in a
CC caspase-3/caspase-8-mediated manner, but also in a caspase-independent
CC manner where mitochondrial apoptosis-inducing factor (AIFM1)
CC translocates to the nucleus (PubMed:23316255). Another study found
CC mature, native (lipidated) protein did not induce apoptosis in THP-1
CC macrophage cell line (PubMed:12874328). Functions as an adhesin, binds
CC to human and mouse macrophages (PubMed:25359607).
CC {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:11160304,
CC ECO:0000269|PubMed:11441098, ECO:0000269|PubMed:12594264,
CC ECO:0000269|PubMed:12874328, ECO:0000269|PubMed:16177361,
CC ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:21078852,
CC ECO:0000269|PubMed:23316255, ECO:0000269|PubMed:25359607,
CC ECO:0000269|PubMed:25504154}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25041568,
CC ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:1906192}. Secreted, cell
CC wall {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:16098710}. Cell
CC surface {ECO:0000269|PubMed:25041568, ECO:0000269|PubMed:25359607}.
CC Secreted {ECO:0000269|PubMed:16098710, ECO:0000305|PubMed:1906192}.
CC Extracellular vesicle, bacterial extracellular vesicle
CC {ECO:0000269|PubMed:21364279}. Host cytoplasm
CC {ECO:0000269|PubMed:11123323}. Note=A soluble cell wall-associated
CC protein (PubMed:10426995). Also found in culture filtrate in increasing
CC quantities during growth (PubMed:1906192, PubMed:16098710). Following
CC infection of mouse macrophage cell line J774A.1 with live (but not
CC heat-killed) bacteria the protein is released in host cytoplasm at 1 hr
CC but decreases dramatically by 3 hrs: release into the host requires
CC protein lipidation and traffics from the immature phagosome through the
CC host class I MHC antigen peptide presentation pathway
CC (PubMed:11123323). Present in bacterial extracytoplasmic vesicles, both
CC in mouse macrophages and in culture media (PubMed:21364279).
CC Immunoelectron microscopy indicates this protein is close to the cell
CC surface (PubMed:25041568). {ECO:0000269|PubMed:10426995,
CC ECO:0000269|PubMed:11123323, ECO:0000269|PubMed:16098710,
CC ECO:0000269|PubMed:1906192, ECO:0000269|PubMed:21364279,
CC ECO:0000269|PubMed:25041568}.
CC -!- INDUCTION: Expressed in cell culture; expressed at a steady level for 4
CC days following infection of human mononuclear phagocytes.
CC {ECO:0000269|PubMed:16177361}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
CC cavity. {ECO:0000305|Ref.25}.
CC -!- DOMAIN: A fragment of the mature protein (residues 41-60) prevents
CC uptake of M.tuberculosis by a human macrophage-like cell line; lesser
CC effects are seen on bacterial uptake by a human lung epithelial cell
CC line. {ECO:0000269|PubMed:25041568}.
CC -!- PTM: Triacylated with a thioether-linked diacylglycerol with C16 and
CC C19 on Cys-22 and an amide-linked C16 fatty acid (PubMed:24093492).
CC Modified by Lgt on Cys-22 with an S-linked diacylglycerol with a
CC mixture of C16, C18 and C19 fatty acids (palmitic, stearic and
CC tuberculostearic acid), signal peptide is removed by LspA, modifed by
CC Lnt with an amide-linked mixture of C16 and C19 fatty acids, expressed
CC in M.bovis (PubMed:24093492). Upon expression in M.smegmatis the
CC protein is glycosylated (possibly by mannose, detected by concanavalin
CC A (conA) binding) within the first 20 residues of the mature protein;
CC altering the probably glycosylated Thr residues alters processing of
CC the mature protein in M.smegmatis and slightly differently in M.vaccae
CC (PubMed:8670858). Glycosylation may protect this region of the protein
CC from proteolysis, which would release the lipoprotein from the cell
CC surface (PubMed:8670858). Mannosylated upon expression in M.smegmatis;
CC treatment with alpha-D-mannosidase decreases its apparent molecular
CC weight (PubMed:16098710). Native protein binds conA (PubMed:16098710).
CC {ECO:0000269|PubMed:16098710, ECO:0000269|PubMed:24093492,
CC ECO:0000269|PubMed:8670858}.
CC -!- MASS SPECTROMETRY: Mass=17300; Method=MALDI; Note=Expressed in M.bovis,
CC lipidated.; Evidence={ECO:0000269|PubMed:24093492};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in culture. Grows less well
CC than wild-type in human monocyte-derived macrophages (MDM) over 7 days;
CC increased human monocyte MHC class II expression, decreased interleukin
CC 1-beta secretion from monocytes and MDM (PubMed:16177361). No growth in
CC C57BL/6 mice over 40 days, even in mice lacking gamma interferon
CC (PubMed:17804126). {ECO:0000269|PubMed:16177361,
CC ECO:0000269|PubMed:17804126}.
CC -!- BIOTECHNOLOGY: A disrupted strain immunizes mice against subsequent
CC infection with wild-type H37Rv as well as the M.bovis vaccine strain
CC BCG. {ECO:0000269|PubMed:17804126}.
CC -!- SIMILARITY: Belongs to the mycobacterial 19 kDa antigen family.
CC {ECO:0000305}.
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DR EMBL; X07945; CAA30766.1; -; Genomic_DNA.
DR EMBL; J03838; AAA25353.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46590.1; -; Genomic_DNA.
DR PIR; D70801; D70801.
DR RefSeq; NP_218280.1; NC_000962.3.
DR RefSeq; WP_003420544.1; NZ_NVQJ01000009.1.
DR PDB; 4ZJM; X-ray; 2.85 A; A/B/C/D/E/F/G=48-159.
DR PDB; 7FDS; X-ray; 1.26 A; A/B=48-159.
DR PDBsum; 4ZJM; -.
DR PDBsum; 7FDS; -.
DR AlphaFoldDB; P9WK61; -.
DR SMR; P9WK61; -.
DR STRING; 83332.Rv3763; -.
DR PaxDb; P9WK61; -.
DR GeneID; 45427763; -.
DR GeneID; 886097; -.
DR KEGG; mtu:Rv3763; -.
DR TubercuList; Rv3763; -.
DR eggNOG; ENOG502ZGGY; Bacteria.
DR OMA; CSDMGGN; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0046789; F:host cell surface receptor binding; IPI:MTBBASE.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MTBBASE.
DR GO; GO:0052553; P:modulation by symbiont of host immune response; IMP:MTBBASE.
DR GO; GO:0052151; P:positive regulation by symbiont of host apoptotic process; IDA:UniProtKB.
DR InterPro; IPR008691; LpqH.
DR Pfam; PF05481; Myco_19_kDa; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Disulfide bond; Glycoprotein;
KW Host cytoplasm; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Secreted; Signal; Transport; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000305"
FT CHAIN 22..159
FT /note="Lipoprotein LpqH"
FT /id="PRO_0000018128"
FT REGION 24..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..60
FT /note="Prevents bacterial uptake by a human macrophage-like
FT cell line"
FT /evidence="ECO:0000269|PubMed:25041568"
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:0000305|PubMed:1906192,
FT ECO:0000305|PubMed:24093492"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:24093492"
FT DISULFID 67..158
FT /evidence="ECO:0007744|PDB:4ZJM"
FT MUTAGEN 1..22
FT /note="MKRGLTVAVAGAAILVAGLSGC->M: Protein not exported from
FT cytoplasm, not released into host cytoplasm (uses
FT recombinant M.vaccae to infect mouse macrophages)."
FT /evidence="ECO:0000269|PubMed:11123323"
FT MUTAGEN 22
FT /note="C->A: Protein not released into host cytoplasm (uses
FT recombinant M.vaccae to infect mouse macrophages)."
FT /evidence="ECO:0000269|PubMed:11123323"
FT MUTAGEN 34..41
FT /note="TTTAAGTT->VVVAAGVV: No ConA binding; altered protein
FT processing yields 16 kDa soluble form starting on residue
FT 40 in M.smegmatis. Protein poorly released into host
FT cytoplasm (uses recombinant M.vaccae to infect mouse
FT macrophages)."
FT /evidence="ECO:0000269|PubMed:11123323,
FT ECO:0000269|PubMed:8670858"
FT MUTAGEN 34..36
FT /note="TTT->VVV: Decreased ConA binding; altered protein
FT processing yields 21 and 17 kDa forms in M.smegmatis."
FT /evidence="ECO:0000269|PubMed:8670858"
FT MUTAGEN 40..41
FT /note="TT->VV: Decreased ConA binding; altered protein
FT processing yields 21 and 16 kDa forms in M.smegmatis."
FT /evidence="ECO:0000269|PubMed:8670858"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:7FDS"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7FDS"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:7FDS"
SQ SEQUENCE 159 AA; 15147 MW; CB1A5090E14867BB CRC64;
MKRGLTVAVA GAAILVAGLS GCSSNKSTTG SGETTTAAGT TASPGAASGP KVVIDGKDQN
VTGSVVCTTA AGNVNIAIGG AATGIAAVLT DGNPPEVKSV GLGNVNGVTL GYTSGTGQGN
ASATKDGSHY KITGTATGVD MANPMSPVNK SFEIEVTCS
