LPPX_MYCTU
ID LPPX_MYCTU Reviewed; 233 AA.
AC P9WK65; L0TCQ0; P65306; P96286;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Putative phthiocerol dimycocerosate transporter LppX {ECO:0000303|PubMed:16541102};
DE AltName: Full=Lipoprotein LppX;
DE Flags: Precursor;
GN Name=lppX; OrderedLocusNames=Rv2945c; ORFNames=MTCY24G1.04;
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 SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
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).
RN [3]
RP DIACYLGLYCEROL AT CYS-27, PALMITOYLATION AT CYS-27, LIPIDATION, SUBCELLULAR
RP LOCATION, AND EXPRESSION IN M.SMEGMATIS.
RX PubMed=19661058; DOI=10.1074/jbc.m109.022715;
RA Tschumi A., Nai C., Auchli Y., Hunziker P., Gehrig P., Keller P., Grau T.,
RA Sander P.;
RT "Identification of apolipoprotein N-acyltransferase (Lnt) in
RT mycobacteria.";
RL J. Biol. Chem. 284:27146-27156(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-27, PALMITOYLATION AT CYS-27,
RP LIPIDATION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND EXPRESSION IN M.BOVIS.
RC STRAIN=H37Rv;
RX PubMed=24093492; DOI=10.1186/1471-2180-13-223;
RA Bruelle J.K., Tschumi A., Sander P.;
RT "Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are
RT N-acylated by apolipoprotein N-acyltransferase BCG_2070c.";
RL BMC Microbiol. 13:223-223(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 27-233, POSSIBLE FUNCTION,
RP DOMAIN, ACYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Mt103;
RX PubMed=16541102; DOI=10.1038/sj.emboj.7601048;
RA Sulzenbacher G., Canaan S., Bordat Y., Neyrolles O., Stadthagen G.,
RA Roig-Zamboni V., Rauzier J., Maurin D., Laval F., Daffe M., Cambillau C.,
RA Gicquel B., Bourne Y., Jackson M.;
RT "LppX is a lipoprotein required for the translocation of phthiocerol
RT dimycocerosates to the surface of Mycobacterium tuberculosis.";
RL EMBO J. 25:1436-1444(2006).
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:0000305|PubMed:16541102}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:10678905}.
CC Secreted, cell wall {ECO:0000269|PubMed:10678905}. Secreted
CC {ECO:0000269|PubMed:10678905}. Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:10678905}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:24093492,
CC ECO:0000305|PubMed:19661058}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
CC cavity (2835 Angstroms(3)) which is large enough to hold a single
CC phthiocerol dimycocerosate (PDIM) molecule.
CC {ECO:0000305|PubMed:16541102}.
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, expressed in M.bovis
CC and M.smegmatis (PubMed:19661058, PubMed:24093492). Hexose glycosylated
CC in N-terminus between residues 27 and 55; there may be 2 sugar moieties
CC in this region, expressed in M.bovis (PubMed:24093492).
CC {ECO:0000269|PubMed:24093492, ECO:0000305|PubMed:19661058}.
CC -!- MASS SPECTROMETRY: Mass=26300; Method=MALDI; Note=Expressed in M.bovis,
CC lipidated and glycosylated.; Evidence={ECO:0000269|PubMed:24093492};
CC -!- DISRUPTION PHENOTYPE: No growth phenotype when grown in culture, no
CC release of phthiocerol dimycocerosates (PDIM) to the culture filtrate.
CC Attenuated virulence, about 80-fold less recovery of bacteria from
CC lungs of 3 week infected BALB/c mice. {ECO:0000269|PubMed:16541102}.
CC -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45749.1; -; Genomic_DNA.
DR PIR; F70668; F70668.
DR RefSeq; NP_217461.1; NC_000962.3.
DR RefSeq; WP_003414872.1; NZ_NVQJ01000015.1.
DR PDB; 2BYO; X-ray; 2.15 A; A=27-233.
DR PDBsum; 2BYO; -.
DR AlphaFoldDB; P9WK65; -.
DR SMR; P9WK65; -.
DR STRING; 83332.Rv2945c; -.
DR PaxDb; P9WK65; -.
DR DNASU; 887956; -.
DR GeneID; 45426931; -.
DR GeneID; 887956; -.
DR KEGG; mtu:Rv2945c; -.
DR TubercuList; Rv2945c; -.
DR eggNOG; ENOG5032I98; Bacteria.
DR OMA; FDDWTNL; -.
DR PhylomeDB; P9WK65; -.
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:0009274; C:peptidoglycan-based cell wall; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005319; F:lipid transporter activity; IDA:MTBBASE.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE.
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 3D-structure; Cell membrane; Cell wall; Glycoprotein; Lipid transport;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Secreted; Signal;
KW Transport; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:24093492"
FT CHAIN 27..233
FT /note="Putative phthiocerol dimycocerosate transporter
FT LppX"
FT /id="PRO_0000018121"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:24093492,
FT ECO:0000305|PubMed:19661058"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:24093492,
FT ECO:0000305|PubMed:19661058"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:2BYO"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2BYO"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:2BYO"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2BYO"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:2BYO"
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
