ID W6T3R3_9LACO Unreviewed; 272 AA.
AC W6T3R3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000256|HAMAP-Rule:MF_01147};
DE EC=2.5.1.145 {ECO:0000256|HAMAP-Rule:MF_01147};
GN Name=lgt {ECO:0000256|HAMAP-Rule:MF_01147};
GN ORFNames=LFAB_17185 {ECO:0000313|EMBL:ETY72511.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY72511.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY72511.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY72511.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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:0000256|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:0000256|HAMAP-Rule:MF_01147};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000256|HAMAP-Rule:MF_01147}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000256|ARBA:ARBA00007150,
CC ECO:0000256|HAMAP-Rule:MF_01147}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETY72511.1}.
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DR EMBL; AWWK01000096; ETY72511.1; -; Genomic_DNA.
DR RefSeq; WP_033615027.1; NZ_KK036541.1.
DR AlphaFoldDB; W6T3R3; -.
DR STRING; 1400520.LFAB_17185; -.
DR PATRIC; fig|1400520.3.peg.3381; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_0_1_9; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000019247; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 NCBIfam; TIGR00544; lgt; 1.
DR PANTHER; PTHR30589:SF0; PHOSPHATIDYLGLYCEROL--PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE; 1.
DR PANTHER; PTHR30589; PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE; 1.
DR Pfam; PF01790; LGT; 1.
DR PROSITE; PS01311; LGT; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Glycosyltransferase {ECO:0000313|EMBL:ETY72511.1};
KW Lipoprotein {ECO:0000313|EMBL:ETY72511.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:ETY72511.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 235..253
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 137
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
SQ SEQUENCE 272 AA; 30901 MW; C9CA45736D044E03 CRC64;
MDLALSSIDT VALRLGPLRI RWYALIIVAG MLIGIWLASK EAPRRHLTTD DITDFMIWAV
PFSLIGVRTY YVLFEWGYYK QHPNEIIALW EGGGAIYGGL IAGTIVLLIF SYRKKINPLD
LLDVAIPGVL LGQSIGRWGN FVNQEAYGAI TTNLNWLPEV FRKQMFISGS YRQPTFLFES
MGTLLGFIIV ILLRHRIKGL LRGEIFGFYL VWYGLLRFVI EGMRTDSLMV GSVRISQLLS
LGLFITGLIF ILYRRFGVRK IDLYNGAALH EN
//