LPRI_MYCTU
ID LPRI_MYCTU Reviewed; 197 AA.
AC P9WK41; L0T8K2; P65318; Q10785;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Lipoprotein LprI {ECO:0000303|PubMed:26589796};
DE AltName: Full=Glycolipoprotein LprI {ECO:0000305};
DE AltName: Full=Lysozyme inhibitor LprI {ECO:0000303|PubMed:26589796};
DE Flags: Precursor;
GN Name=lprI; OrderedLocusNames=Rv1541c; ORFNames=MTCY48.24;
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 [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 [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, LIPIDATION,
RP GLYCOSYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-24; THR-28 AND
RP THR-117.
RC STRAIN=ATCC 25177 / H37Ra, and H37Rv;
RX PubMed=26589796; DOI=10.1074/jbc.m115.662593;
RA Sethi D., Mahajan S., Singh C., Lama A., Hade M.D., Gupta P., Dikshit K.L.;
RT "Lipoprotein LprI of Mycobacterium tuberculosis acts as a lysozyme
RT inhibitor.";
RL J. Biol. Chem. 291:2938-2953(2016).
CC -!- FUNCTION: Strongly binds and inhibits lysozyme, may help bacteria
CC survive in lysozyme-producing host cells. When overexpressed in
CC M.tuberculosis or M.smegmatis increases resistance to hen egg white
CC lysozyme. M.smegmatis overexpressing LprI survive better during
CC intracellular infection of peritoneal and monocyte-derived macrophages,
CC both of which produce lysozyme during infection; M.smegmatis does not
CC encode this protein. Somewhat better survival is seen in human cell
CC lines when M.smegmatis cells express both proteins from this operon,
CC i.e. GlbN (HbN) and LprI. {ECO:0000269|PubMed:26589796}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:26589796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:26589796}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26589796}.
CC Secreted, cell wall {ECO:0000269|PubMed:26589796}. Cell surface
CC {ECO:0000269|PubMed:26589796}. Note=Protein is accessible to externally
CC added trypsin and alpha-D-mannosidase. {ECO:0000269|PubMed:26589796}.
CC -!- INDUCTION: Constitutively expressed, increases in stationary phase (at
CC protein level). mRNA levels rise nearly 50-fold during mouse macrophage
CC infection. Part of the glbN-lprI operon. {ECO:0000269|PubMed:26589796}.
CC -!- PTM: Glycosylated; alpha-D-mannosidase treatment decreases its apparent
CC molecular weight. Glycosylation probably helps target protein to the
CC cell surface; mutation of predicted glycosylation sites (Thr-24, Thr-28
CC and/or Thr-117) makes protein partially inaccesible to externally added
CC trypsin. May also be glycosylated on other residues. Glycosylation is
CC probably not necessary for inhibition of lysozyme.
CC {ECO:0000269|PubMed:26589796}.
CC -!- DISRUPTION PHENOTYPE: Probably essential, it cannot be deleted.
CC {ECO:0000269|PubMed:26589796}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MliC family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44305.1; -; Genomic_DNA.
DR PIR; B70761; B70761.
DR RefSeq; NP_216057.1; NC_000962.3.
DR RefSeq; WP_003407725.1; NZ_NVQJ01000004.1.
DR AlphaFoldDB; P9WK41; -.
DR SMR; P9WK41; -.
DR STRING; 83332.Rv1541c; -.
DR PaxDb; P9WK41; -.
DR DNASU; 886406; -.
DR GeneID; 45425524; -.
DR GeneID; 886406; -.
DR KEGG; mtu:Rv1541c; -.
DR TubercuList; Rv1541c; -.
DR eggNOG; COG4461; Bacteria.
DR OMA; NECWKSE; -.
DR PhylomeDB; P9WK41; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.40.128.200; -; 1.
DR InterPro; IPR009739; LprI_N.
DR InterPro; IPR018660; MliC.
DR InterPro; IPR036328; MliC_sf.
DR Pfam; PF07007; LprI; 1.
DR Pfam; PF09864; MliC; 1.
DR SUPFAM; SSF141488; SSF141488; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..197
FT /note="Lipoprotein LprI"
FT /id="PRO_0000018150"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 24
FT /note="T->A: Decreased apparent weight in M.smegmatis, a
FT portion of the protein is protected from extracellular
FT trypsin."
FT /evidence="ECO:0000269|PubMed:26589796"
FT MUTAGEN 28
FT /note="T->A: Decreased apparent weight in M.smegmatis, a
FT portion of the protein is protected from extracellular
FT trypsin."
FT /evidence="ECO:0000269|PubMed:26589796"
FT MUTAGEN 117
FT /note="T->A: Decreased apparent weight in M.smegmatis, a
FT portion of the protein is protected from extracellular
FT trypsin."
FT /evidence="ECO:0000269|PubMed:26589796"
SQ SEQUENCE 197 AA; 21624 MW; 91461C1E436778BF CRC64;
MRWIGVLVTA LVLSACAANP PANTTSPTAG QSLDCTKPAT IVQQLVCHDR QLTSLDHRLS
TAYQQALAHR RSAALEAAQS SWTMLRDACA QDTDPRTCVQ EAYQTRLVQL AIADPATATP
PVLTYRCPTQ DGPLTAQFYN QFDPKTAVLN WKGDQVIVFV ELSGSGARYG RQGIEYWEHQ
GEVRLDFHGA TFVCRTS
