LGT_BIFAA
ID LGT_BIFAA Reviewed; 336 AA.
AC A1A1J0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147};
DE EC=2.5.1.145 {ECO:0000255|HAMAP-Rule:MF_01147};
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147}; OrderedLocusNames=BAD_0792;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of the diacylglyceryl group from
CC phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine
CC of a prolipoprotein, the first step in the formation of mature
CC lipoproteins. {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-
CC cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate;
CC Xref=Rhea:RHEA:56712, Rhea:RHEA-COMP:14679, Rhea:RHEA-COMP:14680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:140658; EC=2.5.1.145;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01147};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01147};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
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DR EMBL; AP009256; BAF39573.1; -; Genomic_DNA.
DR RefSeq; WP_011743173.1; NC_008618.1.
DR AlphaFoldDB; A1A1J0; -.
DR SMR; A1A1J0; -.
DR STRING; 1680.BADO_0841; -.
DR EnsemblBacteria; BAF39573; BAF39573; BAD_0792.
DR KEGG; bad:BAD_0792; -.
DR HOGENOM; CLU_013386_2_0_11; -.
DR OMA; FRLNPLW; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000008702; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01147; Lgt; 1.
DR InterPro; IPR001640; Lgt.
DR PANTHER; PTHR30589; PTHR30589; 1.
DR Pfam; PF01790; LGT; 1.
DR TIGRFAMs; TIGR00544; lgt; 1.
DR PROSITE; PS01311; LGT; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..336
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_1000137403"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT BINDING 141
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
SQ SEQUENCE 336 AA; 36991 MW; 814690FC3D6BB5CA CRC64;
MTLAYIPSPT ISQFSIGPVT IHFYALCILL GIVLAVWMTT VHWKRYGGNF DQILDITLVA
VPSGIIGARI YHIITTPERF FGPTGDWVEM FRIWNGGLGI WGGVLLGALA AWAWCRHKHY
PMALLGDAVA PGLLVAQAVG RLGNWFNQEL YGAPTTLPWG LKLNMEGSAI GHSEQCYDGA
TCPTGTLFHP TFLYEMIWNL IGAALIVFLG SKIMKKLKAG SLFAIYIMWY TVGRTWIEAL
RIDFAHEFLG VRINVWVSMA VFVLGVVAFI VIQQMGKSTE LLAEKLRTVT EIELSLVEDG
ETGLPTAKAN LTKTKDEITA NDGSSVSYAD DQSDNK