ID   LPPX_MYCBP              Reviewed;         233 AA.
AC   A0A0H3MGR5; Q9RDW1;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Putative phthiocerol dimycocerosate transporter LppX;
DE   AltName: Full=Lipoprotein LppX;
DE   Flags: Precursor;
GN   Name=lppX; OrderedLocusNames=BCG_2967c;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-233, SUBCELLULAR LOCATION, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=BCG;
RX   PubMed=10678905; DOI=10.1128/iai.68.3.1040-1047.2000;
RA   Lefevre P., Denis O., De Wit L., Tanghe A., Vandenbussche P., Content J.,
RA   Huygen K.;
RT   "Cloning of the gene encoding a 22-kilodalton cell surface antigen of
RT   Mycobacterium bovis BCG and analysis of its potential for DNA vaccination
RT   against tuberculosis.";
RL   Infect. Immun. 68:1040-1047(2000).
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, ECO:0000269|PubMed:10678905}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}. Cell surface
CC       {ECO:0000269|PubMed:10678905}. Secreted, cell wall
CC       {ECO:0000269|PubMed:10678905}. Secreted {ECO:0000269|PubMed:10678905}.
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   -!- BIOTECHNOLOGY: Immunizing C57BL/6 and C3H mice with DNA encoding the
CC       mature protein induces antibody production after 3 weeks and stimulates
CC       cytokine production by mouse spleen cells; it does not however protect
CC       mice against infection 8 weeks later with M.tuberculosis H37Rv.
CC       {ECO:0000269|PubMed:10678905}.
CC   -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AM408590; CAL72956.1; -; Genomic_DNA.
DR   EMBL; AJ238176; CAB65225.1; -; Genomic_DNA.
DR   RefSeq; WP_003414872.1; NC_008769.1.
DR   AlphaFoldDB; A0A0H3MGR5; -.
DR   SMR; A0A0H3MGR5; -.
DR   GeneID; 45426931; -.
DR   KEGG; mbb:BCG_2967c; -.
DR   HOGENOM; CLU_1198710_0_0_11; -.
DR   OMA; FDDWTNL; -.
DR   Proteomes; UP000001472; 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   1: Evidence at protein level;
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_0000434586"
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"
FT   CONFLICT        122
FT                   /note="L -> T (in Ref. 2; CAB65225)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="L -> R (in Ref. 2; CAB65225)"
FT                   /evidence="ECO:0000305"
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