LPRF_MYCTU
ID LPRF_MYCTU Reviewed; 261 AA.
AC P9WK47; L0T6N3; P65314; P71798;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Putative diacylated glycolipid transporter LprF;
DE AltName: Full=Lipoprotein LprF;
DE Flags: Precursor;
GN Name=lprF; OrderedLocusNames=Rv1368; ORFNames=MTCY02B12.02;
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 FUNCTION, POSSIBLE INTERACTION WITH KDPD, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND MUTAGENESIS OF MET-132; THR-185 AND ILE-197.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12581360; DOI=10.1046/j.1365-2958.2003.03356.x;
RA Steyn A.J., Joseph J., Bloom B.R.;
RT "Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD
RT with members of the Lpr family.";
RL Mol. Microbiol. 47:1075-1089(2003).
RN [3]
RP DIACYLGLYCEROL AT CYS-39, PALMITOYLATION AT CYS-39, LIPIDATION,
RP GLYCOSYLATION, AND EXPRESSION IN M.SMEGMATIS.
RX PubMed=19944079; DOI=10.1016/j.bbrc.2009.11.120;
RA Bruelle J.K., Grau T., Tschumi A., Auchli Y., Burri R., Polsfuss S.,
RA Keller P.M., Hunziker P., Sander P.;
RT "Cloning, expression and characterization of Mycobacterium tuberculosis
RT lipoprotein LprF.";
RL Biochem. Biophys. Res. Commun. 391:679-684(2010).
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-39, PALMITOYLATION AT CYS-39,
RP LIPIDATION, GLYCOSYLATION, 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).
CC -!- FUNCTION: Might be involved in transporting short diacylated
CC glycolipids to the cell outer membrane (By similarity). Overexpression
CC induces expression of sensor protein kdpD gene at low K(+)
CC concentrations (0 and 250 uM, tested in M.smegatis).
CC {ECO:0000250|UniProtKB:P65315, ECO:0000269|PubMed:12581360}.
CC -!- SUBUNIT: May interact with sensor protein KdpD.
CC {ECO:0000305|PubMed:12581360}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12581360};
CC Lipid-anchor {ECO:0000305}; Extracellular side
CC {ECO:0000305|PubMed:12581360}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a small hydrophobic
CC cavity which is large enough to hold a single diacylated glycolipid
CC molecule. {ECO:0000250|UniProtKB:P65315}.
CC -!- PTM: Modified by Lgt on Cys-39 with an S-linked diacylglycerol with a
CC mixture of C16, C18 and C19 fatty acids (palmitic, stearic and
CC tuberculostearic acid respectively), signal peptide is removed by LspA,
CC modified by Lnt with an amide-linked mixture of C16 and C19 fatty
CC acids, expressed in M.bovis (PubMed:24093492). Hexose glycosylated in
CC N-terminus between residues 39 and 63 (PubMed:24093492).
CC {ECO:0000269|PubMed:19944079, ECO:0000269|PubMed:24093492}.
CC -!- MASS SPECTROMETRY: Mass=29400; Method=MALDI; Note=Expressed in M.bovis,
CC lipidated and glycosylated.; Evidence={ECO:0000269|PubMed:24093492};
CC -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44127.1; -; Genomic_DNA.
DR PIR; E70957; E70957.
DR RefSeq; NP_215884.1; NC_000962.3.
DR RefSeq; WP_003407180.1; NZ_NVQJ01000031.1.
DR AlphaFoldDB; P9WK47; -.
DR SMR; P9WK47; -.
DR STRING; 83332.Rv1368; -.
DR PaxDb; P9WK47; -.
DR DNASU; 886798; -.
DR GeneID; 886798; -.
DR KEGG; mtu:Rv1368; -.
DR TubercuList; Rv1368; -.
DR eggNOG; ENOG50338Y0; Bacteria.
DR OMA; NADVTNQ; -.
DR PhylomeDB; P9WK47; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Lipid transport; Lipid-binding; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..38
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24093492"
FT CHAIN 39..261
FT /note="Putative diacylated glycolipid transporter LprF"
FT /id="PRO_0000018143"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 39
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:19944079,
FT ECO:0000269|PubMed:24093492"
FT LIPID 39
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:19944079,
FT ECO:0000269|PubMed:24093492"
FT MUTAGEN 132
FT /note="M->T: No longer increases KdpD induction at 0 and
FT 250 uM K(+); when associated with S-185 and V-197."
FT /evidence="ECO:0000269|PubMed:12581360"
FT MUTAGEN 185
FT /note="T->S: No longer increases KdpD induction at 0 and
FT 250 uM K(+); when associated with T-132 and V-197."
FT /evidence="ECO:0000269|PubMed:12581360"
FT MUTAGEN 197
FT /note="I->V: No longer increases KdpD induction at 0 and
FT 250 uM K(+); when associated with T-132 and S-185."
FT /evidence="ECO:0000269|PubMed:12581360"
SQ SEQUENCE 261 AA; 26852 MW; 26F99D39A9B756C1 CRC64;
MNGLISQACG SHRPRRPSSL GAVAILIAAT LFATVVAGCG KKPTTASSPS PGSPSPEAQQ
ILQDSSKATK GLHSVHVVVT VNNLSTLPFE SVDADVTNQP QGNGQAVGNA KVRMKPNTPV
VATEFLVTNK TMYTKRGGDY VSVGPAEKIY DPGIILDKDR GLGAVVGQVQ NPTIQGRDAI
DGLATVKVSG TIDAAVIDPI VPQLGKGGGR LPITLWIVDT NASTPAPAAN LVRMVIDKDQ
GNVDITLSNW GAPVTIPNPA G
