ID G1WE73_9BACT Unreviewed; 289 AA.
AC G1WE73;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=HMPREF9431_02203 {ECO:0000313|EMBL:EGV29451.1};
OS Segatella oulorum F0390.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV29451.1, ECO:0000313|Proteomes:UP000005141};
RN [1] {ECO:0000313|EMBL:EGV29451.1, ECO:0000313|Proteomes:UP000005141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0390 {ECO:0000313|EMBL:EGV29451.1,
RC ECO:0000313|Proteomes:UP000005141};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oulorum F0390.";
RL Submitted (JUL-2011) 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: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:EGV29451.1}.
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DR EMBL; ADGI01000062; EGV29451.1; -; Genomic_DNA.
DR RefSeq; WP_004381290.1; NZ_JH114217.1.
DR AlphaFoldDB; G1WE73; -.
DR PATRIC; fig|702438.4.peg.2313; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_10; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000005141; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Lipoprotein {ECO:0000313|EMBL:EGV29451.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000005141};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:EGV29451.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 169
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 289 AA; 33571 MW; D15C5F2868F930A4 CRC64;
MTTLLNYIVW NPNVYLIQVG HWGLRWYSAC WLLGLLGAYF MVKWLFYHQH IAEKTVFVGG
KKQVVNVFDP LFIYCFLGIL IGARLGHCLF YQPDYFLSSG THFIEMLIPY HKMPDGSWQF
VGYEGLASHG GTLGLMIALW LYCRKTGVKL WQVLDDIALA TPITACFIRL GNLMNSEIIG
KVTDVPWAFI FERVDQHPRH PGQLYEALAY ALFFFVGWYF YRVRKQAVGK GFYFGLCITL
IFVFRFFIEY TKDVQVDFES GMLLNMGQLL SVPFVVLGIY CMWRAKQQK
//
