ID A0A149VQL2_9PROT Unreviewed; 264 AA.
AC A0A149VQL2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:KXW55521.1};
GN ORFNames=FV185_12890 {ECO:0000313|EMBL:KXW55521.1};
OS Ferrovum sp. PN-J185.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=1356306 {ECO:0000313|EMBL:KXW55521.1, ECO:0000313|Proteomes:UP000075387};
RN [1] {ECO:0000313|EMBL:KXW55521.1, ECO:0000313|Proteomes:UP000075387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN-J185 {ECO:0000313|EMBL:KXW55521.1,
RC ECO:0000313|Proteomes:UP000075387};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain PN-
RT J185.";
RL Submitted (JAN-2016) 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:KXW55521.1}.
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DR EMBL; LQZA01000003; KXW55521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A149VQL2; -.
DR STRING; 1356306.FV185_12890; -.
DR PATRIC; fig|1356306.3.peg.1279; -.
DR InParanoid; A0A149VQL2; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000075387; 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:KXW55521.1};
KW Lipoprotein {ECO:0000313|EMBL:KXW55521.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000075387};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:KXW55521.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 229..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 140
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 264 AA; 29912 MW; 8B6D29F922CD3A04 CRC64;
MLVHPNFDPV AIHIGPLAVR WYGLMYLFGF LAGSYVGHWR AKTQPWLKWD VDEVDQFLTY
VVFGVVLGGR LGYVLFYKPD YYFSHPLDIF AVWQGGMSFH GGFLGVTIGS MLFARKTQRR
WLEVTDFVAP LVTFGLGFGR LGNFINGELP GRPTSLPWGM VFPQTDLIAR HPSQIYEAIL
EGLVLGTILV IASRRQRPIG VLSSYFLMGY GSFRFLVEFT REPDNFLGLL TFGLSMGQWL
SLPMVIVGIW LWRTSLKSAI IKSE
//
