ID A6DUC8_9BACT Unreviewed; 279 AA.
AC A6DUC8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 13-SEP-2023, entry version 65.
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=LNTAR_02674 {ECO:0000313|EMBL:EDM24752.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM24752.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM24752.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM24752.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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:EDM24752.1}.
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DR EMBL; ABCK01000053; EDM24752.1; -; Genomic_DNA.
DR RefSeq; WP_007281411.1; NZ_ABCK01000053.1.
DR AlphaFoldDB; A6DUC8; -.
DR STRING; 313628.LNTAR_02674; -.
DR eggNOG; COG0682; Bacteria.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000004947; 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:EDM24752.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000004947};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:EDM24752.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 54..73
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 136
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 279 AA; 31258 MW; FF94115453458C44 CRC64;
MKEIFLEFDL FGSQIILRWF QVMAASGFLA ALFLLKKRAK IYGQDPDKIE TTLFYSMIGA
IIGARALFVV RYWDENFANR PFSKIFAFQE GGLVFQGGLI GGLIIAYFIC KRNKINFLTA
LDIAAPCIAL AHAFGRIGCF LNGCCFGGRC SVDAIAVQYP KGSFPWTDHL KRGFIEPQAE
LSAAVHPAPL YSVFALVGVC LLLCYLSKKL AKPGMIFGLY FCVYSLWRII VEFFRDDQDL
TAGLSLAQYI AIGTFLLGCV IIVLCRRNRE LDFPQLEKE
//
