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Lipoprotein LpqH (19 kDa lipoprotein antigen) (Putative transporter LpqH) (p19)

 LPQH_MYCTU              Reviewed;         159 AA.
P9WK61; L0TGP1; P0A5J0; P11572;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 29.
RecName: Full=Lipoprotein LpqH;
AltName: Full=19 kDa lipoprotein antigen;
AltName: Full=Putative transporter LpqH {ECO:0000305|Ref.25};
AltName: Full=p19 {ECO:0000303|PubMed:12594264};
Flags: Precursor;
Name=lpqH; OrderedLocusNames=Rv3763; ORFNames=MTV025.111;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=2493628; DOI=10.1093/nar/17.3.1249;
Ashbridge K.R., Booth R.J., Watson J.D., Lathigra R.B.;
"Nucleotide sequence of the 19 kDa antigen gene from Mycobacterium
tuberculosis.";
Nucleic Acids Res. 17:1249-1249(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3132709; DOI=10.1073/pnas.85.12.4267;
Young D., Lathigra R., Hendrix R., Sweetser D., Young R.A.;
"Stress proteins are immune targets in leprosy and tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 85:4267-4270(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[4]
SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-22.
STRAIN=H37Rv;
PubMed=1906192; DOI=10.1016/0923-2508(91)90097-T;
Young D.B., Garbe T.R.;
"Lipoprotein antigens of Mycobacterium tuberculosis.";
Res. Microbiol. 142:55-65(1991).
[5]
GLYCOSYLATION, EXPRESSION IN M.SMEGMATIS AND M.VACCAE, AND MUTAGENESIS
OF 34-THR--THR-36; 34-THR--THR-41 AND 40-THR-THR-41.
PubMed=8670858;
Herrmann J.L., O'Gaora P., Gallagher A., Thole J.E., Young D.B.;
"Bacterial glycoproteins: a link between glycosylation and proteolytic
cleavage of a 19 kDa antigen from Mycobacterium tuberculosis.";
EMBO J. 15:3547-3554(1996).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=10426995; DOI=10.1126/science.285.5428.732;
Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
"Host defense mechanisms triggered by microbial lipoproteins through
Toll-like receptors.";
Science 285:732-736(1999).
[7]
SUBCELLULAR LOCATION DURING INFECTION, AND MUTAGENESIS OF CYS-22 AND
34-THR--THR-41.
STRAIN=H37Rv;
PubMed=11123323; DOI=10.4049/jimmunol.166.1.447;
Neyrolles O., Gould K., Gares M.P., Brett S., Janssen R., O'Gaora P.,
Herrmann J.L., Prevost M.C., Perret E., Thole J.E., Young D.;
"Lipoprotein access to MHC class I presentation during infection of
murine macrophages with live mycobacteria.";
J. Immunol. 166:447-457(2001).
[8]
FUNCTION IN DENDRITIC CELL MATURATION.
PubMed=11160304; DOI=10.4049/jimmunol.166.4.2444;
Hertz C.J., Kiertscher S.M., Godowski P.J., Bouis D.A., Norgard M.V.,
Roth M.D., Modlin R.L.;
"Microbial lipopeptides stimulate dendritic cell maturation via Toll-
like receptor 2.";
J. Immunol. 166:2444-2450(2001).
[9]
FUNCTION.
STRAIN=ATCC 25177 / H37Ra;
PubMed=11441098; DOI=10.4049/jimmunol.167.2.910;
Noss E.H., Pai R.K., Sellati T.J., Radolf J.D., Belisle J.,
Golenbock D.T., Boom W.H., Harding C.V.;
"Toll-like receptor 2-dependent inhibition of macrophage class II MHC
expression and antigen processing by 19-kDa lipoprotein of
Mycobacterium tuberculosis.";
J. Immunol. 167:910-918(2001).
[10]
FUNCTION IN HOST APOPTOSIS.
PubMed=12594264; DOI=10.4049/jimmunol.170.5.2409;
Lopez M., Sly L.M., Luu Y., Young D., Cooper H., Reiner N.E.;
"The 19-kDa Mycobacterium tuberculosis protein induces macrophage
apoptosis through Toll-like receptor-2.";
J. Immunol. 170:2409-2416(2003).
[11]
FUNCTION IN HOST IFN-G SIGNALING, AND DOES NOT CAUSE HOST APOPTOSIS.
STRAIN=ATCC 25177 / H37Ra;
PubMed=12874328; DOI=10.1128/IAI.71.8.4487-4497.2003;
Gehring A.J., Rojas R.E., Canaday D.H., Lakey D.L., Harding C.V.,
Boom W.H.;
"The Mycobacterium tuberculosis 19-kilodalton lipoprotein inhibits
gamma interferon-regulated HLA-DR and Fc gamma R1 on human macrophages
through Toll-like receptor 2.";
Infect. Immun. 71:4487-4497(2003).
[12]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND EXPRESSION IN M.SMEGMATIS.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=16098710; DOI=10.1016/j.micpath.2005.06.002;
Diaz-Silvestre H., Espinosa-Cueto P., Sanchez-Gonzalez A.,
Esparza-Ceron M.A., Pereira-Suarez A.L., Bernal-Fernandez G.,
Espitia C., Mancilla R.;
"The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin
that binds the mannose receptor of THP-1 monocytic cells and promotes
phagocytosis of mycobacteria.";
Microb. Pathog. 39:97-107(2005).
[13]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=16177361; DOI=10.1128/IAI.73.10.6831-6837.2005;
Stewart G.R., Wilkinson K.A., Newton S.M., Sullivan S.M.,
Neyrolles O., Wain J.R., Patel J., Pool K.L., Young D.B.,
Wilkinson R.J.;
"Effect of deletion or overexpression of the 19-kilodalton lipoprotein
Rv3763 on the innate response to Mycobacterium tuberculosis.";
Infect. Immun. 73:6831-6837(2005).
[14]
FUNCTION.
STRAIN=ATCC 25177 / H37Ra;
PubMed=16622205; DOI=10.1128/IAI.74.5.2686-2696.2006;
Jung S.B., Yang C.S., Lee J.S., Shin A.R., Jung S.S., Son J.W.,
Harding C.V., Kim H.J., Park J.K., Paik T.H., Song C.H., Jo E.K.;
"The mycobacterial 38-kilodalton glycolipoprotein antigen activates
the mitogen-activated protein kinase pathway and release of
proinflammatory cytokines through Toll-like receptors 2 and 4 in human
monocytes.";
Infect. Immun. 74:2686-2696(2006).
[15]
DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
STRAIN=H37Rv;
PubMed=17804126; DOI=10.1016/j.vaccine.2007.07.042;
Henao-Tamayo M., Junqueira-Kipnis A.P., Ordway D.,
Gonzales-Juarrero M., Stewart G.R., Young D.B., Wilkinson R.J.,
Basaraba R.J., Orme I.M.;
"A mutant of Mycobacterium tuberculosis lacking the 19-kDa lipoprotein
Rv3763 is highly attenuated in vivo but retains potent vaccinogenic
properties.";
Vaccine 25:7153-7159(2007).
[16]
FUNCTION.
STRAIN=H37Rv;
PubMed=21078852; DOI=10.1128/IAI.00806-10;
Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H.,
Rojas R.E.;
"Mycobacterium tuberculosis lipoproteins directly regulate human
memory CD4(+) T cell activation via Toll-like receptors 1 and 2.";
Infect. Immun. 79:663-673(2011).
[17]
SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=21364279; DOI=10.1172/JCI44261;
Prados-Rosales R., Baena A., Martinez L.R., Luque-Garcia J.,
Kalscheuer R., Veeraraghavan U., Camara C., Nosanchuk J.D.,
Besra G.S., Chen B., Jimenez J., Glatman-Freedman A., Jacobs W.R. Jr.,
Porcelli S.A., Casadevall A.;
"Mycobacteria release active membrane vesicles that modulate immune
responses in a TLR2-dependent manner in mice.";
J. Clin. Invest. 121:1471-1483(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[19]
FUNCTION IN HOST APOPTOSIS.
PubMed=23316255; DOI=10.1155/2012/950503;
Sanchez A., Espinosa P., Garcia T., Mancilla R.;
"The 19 kDa Mycobacterium tuberculosis lipoprotein (LpqH) induces
macrophage apoptosis through extrinsic and intrinsic pathways: a role
for the mitochondrial apoptosis-inducing factor.";
Clin. Dev. Immunol. 2012:950503-950503(2012).
[20]
MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-22, PALMITOYLATION AT CYS-22,
LIPIDATION, POST-TRANSLATIONAL MODIFICATION, AND EXPRESSION IN
M.BOVIS.
STRAIN=H37Rv;
PubMed=24093492; DOI=10.1186/1471-2180-13-223;
Bruelle J.K., Tschumi A., Sander P.;
"Lipoproteins of slow-growing Mycobacteria carry three fatty acids and
are N-acylated by apolipoprotein N-acyltransferase BCG_2070c.";
BMC Microbiol. 13:223-223(2013).
[21]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=25041568; DOI=10.1111/cbdd.12365;
Ocampo M., Curtidor H., Vanegas M., Patarroyo M.A., Patarroyo M.E.;
"Specific interaction between Mycobacterium tuberculosis lipoprotein-
derived peptides and target cells inhibits mycobacterial entry in
vitro.";
Chem. Biol. Drug Des. 84:626-641(2014).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=H37Rv;
PubMed=25359607; DOI=10.1111/sji.12249;
Esparza M., Palomares B., Garcia T., Espinosa P., Zenteno E.,
Mancilla R.;
"PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an
adhesin, which binds the macrophage mannose receptor and promotes
phagocytosis.";
Scand. J. Immunol. 81:46-55(2015).
[23]
FUNCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=25504154; DOI=10.3892/mmr.2014.3070;
Liu L., Liu J., Niu G., Xu Q., Chen Q.;
"Mycobacterium tuberculosis 19-kDa lipoprotein induces Toll-like
receptor 2-dependent peroxisome proliferator-activated receptor gamma
expression and promotes inflammatory responses in human macrophages.";
Mol. Med. Report. 11:2921-2926(2015).
[24]
REVIEW.
PubMed=20234378; DOI=10.1038/nrmicro2321;
Harding C.V., Boom W.H.;
"Regulation of antigen presentation by Mycobacterium tuberculosis: a
role for Toll-like receptors.";
Nat. Rev. Microbiol. 8:296-307(2010).
[25]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 48-159, PUTATIVE FUNCTION,
DOMAIN, AND DISULFIDE BOND.
STRAIN=H37Rv;
Arbing M.A., Chan S., Kuo E., Harris L.R., Zhou T.T., Eisenberg D.;
"Crystal structure of Mycobacterium tuberculosis LpqH (Rv3763).";
Submitted (APR-2015) to the PDB data bank.
-!- FUNCTION: Based on its structure might be involved in ligand
transport (Ref.25) (By similarity). {ECO:0000250|UniProtKB:P65307,
ECO:0000305|Ref.25}.
-!- FUNCTION: A host TLR2 agonist (PubMed:10426995, PubMed:11441098,
PubMed:12874328). Plays a complicated role in bacterial
interactions with the host immune system; some effects favor the
host (induces interleukin 1-beta and IL-12 p40 (IL12B), both
increase the host's immune response) while others favor the
bacteria (increases growth in monocyte-derived macrophages and
decreases host MHC class II (MHC-II) expression and antigen
processing) (PubMed:16177361). Induces host (human and mouse) IL-
12 p40 (IL12B, a proinflammatory cytokine) release by monocyte
cell lines via TLR2 and CD14 (PubMed:10426995). Induces host
(human) monocytes to produce TNF-alpha, IL-6 and IL-12 p40; LpqH
is a more potent inducer than PstS1 (PubMed:16622205). Inhibits
MHC-II expression and antigen processing in host (mouse)
macrophages via TLR2 (independently of TLR4) probably via the
lipid modification (PubMed:11441098). Stimulates host (human)
dendritic cell maturation to become MHC-II-positive antigen
presenting cells via TLR2, which depends on lipidation;
nonlipidated protein does not stimulate maturation
(PubMed:11160304). Inhibits host (human and mouse) IFN-gamma
signaling in macrophages via TLR2; decreases IFN-gamma stimulated
MHC-II antigen processing as well as decreasing IFN-gamma-mediated
up-regulation of immunoglobulin gamma Fc receptor (FCGR1A),
enabling the bacteria to evade the immune system
(PubMed:12874328). In resting human CD4+ T-cells lipidated (but
probably not nonlipidated protein) is a costimulatory ligand (with
anti-CD3 and anti-CD28) for T-cell proliferation and IFN-gamma and
IL-2 production (PubMed:21078852). Human CD4+ T-cells probably use
TLR1/TLR2 heterodimers to respond to mycobacterial lipoproteins
(PubMed:21078852). Acting via TLR2 enhances expression of host
peroxisome proliferator-activated receptor gamma (PPARG), a
regulator of inflammation and immunoregulation, and increases p38
MAPK phosphorylation, IL-6 and TNF-alpha expression
(PubMed:25504154). Native or nonlipidated recombinant protein
missing the first 4 residues have been shown to induce apoptosis
in the human macrophage cell line THP-1 and human monocyte-derived
macrophages in a TLR2, caspase-3 and caspase-8-dependent manner
(PubMed:12594264). Protein overexpressed in M.smegmatis (lipidated
and probably glycosylated) induces apoptosis in human macrophages
via TLR2 in a caspase-3/caspase-8-mediated manner, but also in a
caspase-independent manner where mitochondrial apoptosis-inducing
factor (AIFM1) translocates to the nucleus (PubMed:23316255).
Another study found mature, native (lipidated) protein did not
induce apoptosis in THP-1 macrophage cell line (PubMed:12874328).
Functions as an adhesin, binds to human and mouse macrophages
(PubMed:25359607). {ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:11160304, ECO:0000269|PubMed:11441098,
ECO:0000269|PubMed:12594264, ECO:0000269|PubMed:12874328,
ECO:0000269|PubMed:16177361, ECO:0000269|PubMed:16622205,
ECO:0000269|PubMed:21078852, ECO:0000269|PubMed:23316255,
ECO:0000269|PubMed:25359607, ECO:0000269|PubMed:25504154}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25041568,
ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:1906192}. Secreted,
cell wall {ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:16098710}. Cell surface
{ECO:0000269|PubMed:25041568, ECO:0000269|PubMed:25359607}.
Secreted {ECO:0000269|PubMed:16098710,
ECO:0000305|PubMed:1906192}. Extracellular vesicle, Bacterial
extracellular vesicle {ECO:0000269|PubMed:21364279}. Host
cytoplasm {ECO:0000269|PubMed:11123323}. Note=A soluble cell wall-
associated protein (PubMed:10426995). Also found in culture
filtrate in increasing quantities during growth (PubMed:1906192,
PubMed:16098710). Following infection of mouse macrophage cell
line J774A.1 with live (but not heat-killed) bacteria the protein
is released in host cytoplasm at 1 hr but decreases dramatically
by 3 hrs: release into the host requires protein lipidation and
traffics from the immature phagosome through the host class I MHC
antigen peptide presentation pathway (PubMed:11123323). Present in
bacterial extracytoplasmic vesicles, both in mouse macrophages and
in culture media (PubMed:21364279). Immunoelectron microscopy
indicates this protein is close to the cell surface
(PubMed:25041568). {ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:11123323, ECO:0000269|PubMed:16098710,
ECO:0000269|PubMed:1906192, ECO:0000269|PubMed:21364279,
ECO:0000269|PubMed:25041568}.
-!- INDUCTION: Expressed in cell culture; expressed at a steady level
for 4 days following infection of human mononuclear phagocytes.
{ECO:0000269|PubMed:16177361}.
-!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
cavity. {ECO:0000305|Ref.25}.
-!- DOMAIN: A fragment of the mature protein (residues 41-60) prevents
uptake of M.tuberculosis by a human macrophage-like cell line;
lesser effects are seen on bacterial uptake by a human lung
epithelial cell line. {ECO:0000269|PubMed:25041568}.
-!- PTM: Triacylated with a thioether-linked diacylglycerol with C16
and C19 on Cys-22 and an amide-linked C16 fatty acid
(PubMed:24093492). Modified by Lgt on Cys-22 with an S-linked
diacylglycerol with a mixture of C16, C18 and C19 fatty acids
(palmitic, stearic and tuberculostearic acid), signal peptide is
removed by LspA, modifed by Lnt with an amide-linked mixture of
C16 and C19 fatty acids, expressed in M.bovis (PubMed:24093492).
Upon expression in M.smegmatis the protein is glycosylated
(possibly by mannose, detected by concanavalin A (conA) binding)
within the first 20 residues of the mature protein; altering the
probably glycosylated Thr residues alters processing of the mature
protein in M.smegmatis and slightly differently in M.vaccae
(PubMed:8670858). Glycosylation may protect this region of the
protein from proteolysis, which would release the lipoprotein from
the cell surface (PubMed:8670858). Mannosylated upon expression in
M.smegmatis; treatment with alpha-D-mannosidase decreases its
apparent molecular weight (PubMed:16098710). Native protein binds
conA (PubMed:16098710). {ECO:0000269|PubMed:16098710,
ECO:0000269|PubMed:24093492, ECO:0000269|PubMed:8670858}.
-!- MASS SPECTROMETRY: Mass=17300; Method=MALDI; Range=22-159;
Note=Expressed in M.bovis, lipidated.;
Evidence={ECO:0000269|PubMed:24093492};
-!- DISRUPTION PHENOTYPE: No visible phenotype in culture. Grows less
well than wild-type in human monocyte-derived macrophages (MDM)
over 7 days; increased human monocyte MHC class II expression,
decreased interleukin 1-beta secretion from monocytes and MDM
(PubMed:16177361). No growth in C57BL/6 mice over 40 days, even in
mice lacking gamma interferon (PubMed:17804126).
{ECO:0000269|PubMed:16177361, ECO:0000269|PubMed:17804126}.
-!- BIOTECHNOLOGY: A disrupted strain immunizes mice against
subsequent infection with wild-type H37Rv as well as the M.bovis
vaccine strain BCG. {ECO:0000269|PubMed:17804126}.
-!- SIMILARITY: Belongs to the mycobacterial 19 kDa antigen family.
{ECO:0000305}.
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EMBL; X07945; CAA30766.1; -; Genomic_DNA.
EMBL; J03838; AAA25353.1; -; Genomic_DNA.
EMBL; AL123456; CCP46590.1; -; Genomic_DNA.
PIR; D70801; D70801.
RefSeq; NP_218280.1; NC_000962.3.
RefSeq; WP_003420544.1; NZ_KK339374.1.
PDB; 4ZJM; X-ray; 2.85 A; A/B/C/D/E/F/G=48-159.
PDBsum; 4ZJM; -.
ProteinModelPortal; P9WK61; -.
SMR; P9WK61; -.
STRING; 83332.Rv3763; -.
PaxDb; P9WK61; -.
EnsemblBacteria; CCP46590; CCP46590; Rv3763.
GeneID; 886097; -.
KEGG; mtu:Rv3763; -.
TubercuList; Rv3763; -.
KO; K14953; -.
OMA; CSDMGGN; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0046789; F:host cell surface receptor binding; IPI:MTBBASE.
GO; GO:0044117; P:growth of symbiont in host; IMP:MTBBASE.
GO; GO:0052553; P:modulation by symbiont of host immune response; IMP:MTBBASE.
GO; GO:0052157; P:modulation by symbiont of microbe-associated molecular pattern-induced host innate immune response; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0052151; P:positive regulation by symbiont of host apoptotic process; IDA:UniProtKB.
InterPro; IPR008691; LpqH.
Pfam; PF05481; Myco_19_kDa; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell wall; Complete proteome;
Disulfide bond; Glycoprotein; Host cytoplasm; Lipoprotein; Membrane;
Palmitate; Reference proteome; Secreted; Signal; Transport; Virulence.
SIGNAL 1 21 {ECO:0000305}.
CHAIN 22 159 Lipoprotein LpqH.
/FTId=PRO_0000018128.
REGION 41 60 Prevents bacterial uptake by a human
macrophage-like cell line.
{ECO:0000269|PubMed:25041568}.
LIPID 22 22 N-palmitoyl cysteine.
{ECO:0000305|PubMed:1906192,
ECO:0000305|PubMed:24093492}.
LIPID 22 22 S-diacylglycerol cysteine.
{ECO:0000305|PubMed:24093492}.
DISULFID 67 158 {ECO:0000244|PDB:4ZJM}.
MUTAGEN 1 22 MKRGLTVAVAGAAILVAGLSGC->M: Protein not
exported from cytoplasm, not released
into host cytoplasm (uses recombinant
M.vaccae to infect mouse macrophages).
{ECO:0000269|PubMed:11123323}.
MUTAGEN 22 22 C->A: Protein not released into host
cytoplasm (uses recombinant M.vaccae to
infect mouse macrophages).
{ECO:0000269|PubMed:11123323}.
MUTAGEN 34 41 TTTAAGTT->VVVAAGVV: No ConA binding;
altered protein processing yields 16 kDa
soluble form starting on residue 40 in
M.smegmatis. Protein poorly released into
host cytoplasm (uses recombinant M.vaccae
to infect mouse macrophages).
{ECO:0000269|PubMed:11123323,
ECO:0000269|PubMed:8670858}.
MUTAGEN 34 36 TTT->VVV: Decreased ConA binding; altered
protein processing yields 21 and 17 kDa
forms in M.smegmatis.
{ECO:0000269|PubMed:8670858}.
MUTAGEN 40 41 TT->VV: Decreased ConA binding; altered
protein processing yields 21 and 16 kDa
forms in M.smegmatis.
{ECO:0000269|PubMed:8670858}.
STRAND 51 54 {ECO:0000244|PDB:4ZJM}.
STRAND 65 70 {ECO:0000244|PDB:4ZJM}.
STRAND 73 78 {ECO:0000244|PDB:4ZJM}.
TURN 81 83 {ECO:0000244|PDB:4ZJM}.
STRAND 85 94 {ECO:0000244|PDB:4ZJM}.
STRAND 97 105 {ECO:0000244|PDB:4ZJM}.
STRAND 108 113 {ECO:0000244|PDB:4ZJM}.
STRAND 116 118 {ECO:0000244|PDB:4ZJM}.
STRAND 120 124 {ECO:0000244|PDB:4ZJM}.
STRAND 129 138 {ECO:0000244|PDB:4ZJM}.
STRAND 141 143 {ECO:0000244|PDB:4ZJM}.
STRAND 148 157 {ECO:0000244|PDB:4ZJM}.
SEQUENCE 159 AA; 15147 MW; CB1A5090E14867BB CRC64;
MKRGLTVAVA GAAILVAGLS GCSSNKSTTG SGETTTAAGT TASPGAASGP KVVIDGKDQN
VTGSVVCTTA AGNVNIAIGG AATGIAAVLT DGNPPEVKSV GLGNVNGVTL GYTSGTGQGN
ASATKDGSHY KITGTATGVD MANPMSPVNK SFEIEVTCS


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