ID   LPPX_MYCTO              Reviewed;         233 AA.
AC   P9WK64; L0TCQ0; P65306; P96286;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Putative phthiocerol dimycocerosate transporter LppX;
DE   AltName: Full=Lipoprotein LppX;
DE   Flags: Precursor;
GN   Name=lppX; OrderedLocusNames=MT3017;
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: 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; AE000516; AAK47344.1; -; Genomic_DNA.
DR   PIR; F70668; F70668.
DR   RefSeq; WP_003414872.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK64; -.
DR   SMR; P9WK64; -.
DR   EnsemblBacteria; AAK47344; AAK47344; MT3017.
DR   GeneID; 45426931; -.
DR   KEGG; mtc:MT3017; -.
DR   PATRIC; fig|83331.31.peg.3258; -.
DR   HOGENOM; CLU_1198710_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-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; 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_0000427708"
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;  24140 MW;  FFACCDB2C7C2E87F CRC64;
     MNDGKRAVTS AVLVVLGACL ALWLSGCSSP KPDAEEQGVP VSPTASDPAL LAEIRQSLDA
     TKGLTSVHVA VRTTGKVDSL LGITSADVDV RANPLAAKGV CTYNDEQGVP FRVQGDNISV
     KLFDDWSNLG SISELSTSRV LDPAAGVTQL LSGVTNLQAQ GTEVIDGIST TKITGTIPAS
     SVKMLDPGAK SARPATVWIA QDGSHHLVRA SIDLGSGSIQ LTQSKWNEPV NVD