ID A0A143WSH6_9ENTR Unreviewed; 288 AA.
AC A0A143WSH6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:CUX96705.1};
GN ORFNames=MHIR_DE00432 {ECO:0000313|EMBL:CUX96705.1};
OS Candidatus Doolittlea endobia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Doolittlea.
OX NCBI_TaxID=1778262 {ECO:0000313|EMBL:CUX96705.1, ECO:0000313|Proteomes:UP000095322};
RN [1] {ECO:0000313|Proteomes:UP000095322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Husnik F.;
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}.
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DR EMBL; LN999833; CUX96705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143WSH6; -.
DR STRING; 1778262.MHIR_DE00432; -.
DR KEGG; den:MHIR_DE00432; -.
DR PATRIC; fig|1778262.3.peg.780; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000095322; Chromosome i.
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:CUX96705.1};
KW Lipoprotein {ECO:0000313|EMBL:CUX96705.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000095322};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:CUX96705.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 13..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 252..279
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 142
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 288 AA; 33161 MW; 450DDFF26FDA5C5F CRC64;
MIHYLACPKF NPVLFSFGLV SLNLYGLMYL VGFIFAMWMA VRRTNHPGSG WTKQEVESLL
YASFWGVFFG GRIGYVLFYN LSLFLDNPFY LFRVWNGGMS FHGGLIGVIV IMLWFSYRTR
RHFFQVADFV SPMVPFGLGA GRLGNFINGE LWGRVTTVPW AMLFPGSMKE DIALLTSNQK
WQVLFERYGM LPRHPSQLYE LFLEGIVLFI ILNLFIRKPR PIGSVSGLFL ICYGAFRVFV
EFFRQPDAQL GLFSDIISMG QILSLPMILA GIIIMIWAYR CRSQRQPL
//
