ID   LPRI_MYCTO              Reviewed;         197 AA.
AC   P9WK40; 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:0000250|UniProtKB:P9WK41};
DE   AltName: Full=Glycolipoprotein LprI;
DE   AltName: Full=Lysozyme inhibitor LprI;
DE   Flags: Precursor;
GN   Name=lprI; OrderedLocusNames=MT1593;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Strongly binds and inhibits lysozyme, may help bacteria
CC       survive in lysozyme-producing host cells such as monocyte-derived
CC       macrophages. {ECO:0000250|UniProtKB:P9WK41}.
CC   -!- SUBUNIT: Probably a homodimer. {ECO:0000250|UniProtKB:P9WK41}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Secreted, cell wall {ECO:0000250|UniProtKB:P9WK41}. Cell surface
CC       {ECO:0000250|UniProtKB:P9WK41}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P9WK41}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MliC family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45859.1; -; Genomic_DNA.
DR   PIR; B70761; B70761.
DR   RefSeq; WP_003407725.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK40; -.
DR   SMR; P9WK40; -.
DR   EnsemblBacteria; AAK45859; AAK45859; MT1593.
DR   GeneID; 45425524; -.
DR   KEGG; mtc:MT1593; -.
DR   PATRIC; fig|83331.31.peg.1714; -.
DR   HOGENOM; CLU_098273_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell membrane; Cell wall; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..197
FT                   /note="Lipoprotein LprI"
FT                   /id="PRO_0000427720"
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"
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