LPRF_MYCTO
ID LPRF_MYCTO Reviewed; 261 AA.
AC P9WK46; L0T6N3; P65314; P71798;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Putative diacylated glycolipid transporter LprF;
DE AltName: Full=Lipoprotein LprF;
DE Flags: Precursor;
GN Name=lprF; OrderedLocusNames=MT1415;
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 transporting short diacylated
CC glycolipids to the cell outer membrane (By similarity).
CC {ECO:0000250|UniProtKB:P65315}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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 acids
CC (By similarity). {ECO:0000250|UniProtKB:P9WK47}.
CC -!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45679.1; -; Genomic_DNA.
DR PIR; E70957; E70957.
DR RefSeq; WP_003407180.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WK46; -.
DR SMR; P9WK46; -.
DR EnsemblBacteria; AAK45679; AAK45679; MT1415.
DR KEGG; mtc:MT1415; -.
DR PATRIC; fig|83331.31.peg.1522; -.
DR HOGENOM; CLU_074100_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cell membrane; Lipid transport; Lipid-binding; Lipoprotein; Membrane;
KW Palmitate; Signal; Transport.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..261
FT /note="Putative diacylated glycolipid transporter LprF"
FT /id="PRO_0000427717"
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:0000255"
FT LIPID 39
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
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