ID   LPPX_MYCLE              Reviewed;         233 AA.
AC   Q9CD80;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Putative phthiocerol dimycocerosate transporter LppX;
DE   AltName: Full=Lipoprotein LppX;
DE   Flags: Precursor;
GN   Name=lppX; OrderedLocusNames=ML0136;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Might be involved in translocating phthiocerol
CC       dimycocerosates (PDIM) from the cell membrane to the outer membrane;
CC       PDIM forms part of the cell wall. {ECO:0000250|UniProtKB:P9WK65}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Cell surface {ECO:0000250|UniProtKB:P9WK65}. Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P9WK65}. Secreted
CC       {ECO:0000250|UniProtKB:P9WK65}.
CC   -!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
CC       cavity which is large enough to hold a single phthiocerol
CC       dimycocerosate (PDIM) molecule. {ECO:0000250|UniProtKB:P9WK65}.
CC   -!- PTM: Modified by Lgt on Cys-27 with an S-linked diacylglycerol with a
CC       mixture of C16 and C19 fatty acids (palmitic and tuberculostearic
CC       acid), signal peptide is removed by LspA, modified by Lnt with an
CC       amide-linked mixture of C16 and C19 fatty acids.
CC       {ECO:0000250|UniProtKB:P9WK65}.
CC   -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AL583917; CAC29644.1; -; Genomic_DNA.
DR   PIR; H86925; H86925.
DR   RefSeq; NP_301230.1; NC_002677.1.
DR   RefSeq; WP_010907555.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD80; -.
DR   SMR; Q9CD80; -.
DR   STRING; 272631.ML0136; -.
DR   EnsemblBacteria; CAC29644; CAC29644; CAC29644.
DR   KEGG; mle:ML0136; -.
DR   PATRIC; fig|272631.5.peg.204; -.
DR   Leproma; ML0136; -.
DR   eggNOG; ENOG5032I98; Bacteria.
DR   HOGENOM; CLU_1198710_0_0_11; -.
DR   OMA; FDDWTNL; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd16334; LppX-like; 1.
DR   InterPro; IPR029046; LolA/LolB/LppX.
DR   InterPro; IPR009830; LppX/LprAFG.
DR   Pfam; PF07161; LppX_LprAFG; 1.
DR   SUPFAM; SSF89392; SSF89392; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall; Lipid transport; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           27..233
FT                   /note="Putative phthiocerol dimycocerosate transporter
FT                   LppX"
FT                   /id="PRO_0000018120"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           27
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           27
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   233 AA;  24411 MW;  A6BAC1269FD4C063 CRC64;
     MNDRKWVTSS VMLVTLSACL ALGLSGCSST KPDAQEQSSS SSPASSDPAL TAEIKQSLET
     TKALSSVHVV VQTTGKVDAL LGISNADVDV QANPLAVKGT CTYNDQPGVP FRVLGDNISV
     KLFDDWSNLG SISDLSTSHV LDPNTGITQV LSGVINLQAQ GTEVVDRIPT NKITGTVPTS
     SVKMLDPKAK GSKLATVWIA QDGSHHLVRA SIDLGSGSIQ LTQSKWNEPV NTN