LPRF_MYCBO
ID LPRF_MYCBO Reviewed; 261 AA.
AC P65315; A0A1R3XY62; P71798; X2BHQ5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Putative diacylated glycolipid transporter LprF {ECO:0000303|PubMed:25286846};
DE AltName: Full=Lipoprotein LprF;
DE Flags: Precursor;
GN Name=lprF; OrderedLocusNames=BQ2027_MB1403;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 40-261, POSSIBLE FUNCTION,
RP SUBUNIT, DOMAIN, POSSIBLE LIPID-BINDING, MUTAGENESIS OF ALA-110, AND
RP EXPRESSION IN M.SMEGMATIS.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=25286846; DOI=10.1107/s1399004714016599;
RA Kim J.S., Jiao L., Oh J.I., Ha N.C., Kim Y.H.;
RT "Crystal structure and functional implications of LprF from Mycobacterium
RT tuberculosis and M. bovis.";
RL Acta Crystallogr. D 70:2619-2630(2014).
CC -!- FUNCTION: Might be involved in transporting short diacylated
CC glycolipids to the cell outer membrane. Binds glycolipids that contain
CC a diacylated glycerophosphate or a diacylated phosphatidylinositol
CC moiety with C14 and C16 chains (upon overexpression in M.smegmatis;
CC M.smegmatis does not encode this gene). Overexpression in M.smegmatis
CC increases the cell wall glycolipid LAM/LM ratio
CC (lipoarabinomannan/lipomannan), suggesting perhaps this protein is
CC involved in the preferential translocation of diacylated LAM to the
CC outer cell membrane. Overexpressing M.smegmatis cells adhere less well
CC to hexadecane droplets, indicating decrease in the hydrophobicity of
CC the cell surface, and have a slightly increased resistance to the
CC antibiotic ethambutol. {ECO:0000305|PubMed:25286846}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:25286846}.
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 (933 Angstroms(3)) which is large enough to hold a single
CC diacylated glycolipid molecule. {ECO:0000305|PubMed:25286846}.
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; LT708304; SIU00007.1; -; Genomic_DNA.
DR RefSeq; NP_855057.1; NC_002945.3.
DR RefSeq; WP_003407180.1; NC_002945.4.
DR PDB; 4QA8; X-ray; 1.10 A; A=40-261.
DR PDBsum; 4QA8; -.
DR AlphaFoldDB; P65315; -.
DR SMR; P65315; -.
DR EnsemblBacteria; SIU00007; SIU00007; BQ2027_MB1403.
DR PATRIC; fig|233413.5.peg.1539; -.
DR OMA; NADVTNQ; -.
DR Proteomes; UP000001419; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipid transport; Lipid-binding; Lipoprotein;
KW Membrane; 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_0000018142"
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"
FT MUTAGEN 110
FT /note="A->Y: Loss of glycolipid-binding, increased cell
FT surface hydrophobicity, loss of slight ethambutol
FT antibiotic resistance."
FT /evidence="ECO:0000269|PubMed:25286846"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:4QA8"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4QA8"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4QA8"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4QA8"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 170..182
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:4QA8"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4QA8"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4QA8"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:4QA8"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:4QA8"
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
