ID S4XXE5_SORCE Unreviewed; 312 AA.
AC S4XXE5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=SCE1572_23450 {ECO:0000313|EMBL:AGP37179.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP37179.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP37179.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP37179.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP37179.1; -; Genomic_DNA.
DR RefSeq; WP_020736617.1; NC_021658.1.
DR AlphaFoldDB; S4XXE5; -.
DR STRING; 1254432.SCE1572_23450; -.
DR KEGG; scu:SCE1572_23450; -.
DR PATRIC; fig|1254432.3.peg.5318; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_2_7; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000014803; Chromosome.
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 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 Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 44..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 247..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 276..298
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 312 AA; 33729 MW; 83E19F6F1AAA61CB CRC64;
MRPELFRLLD VAFPAYFLLL LTGFLFATAI GALWARRIGE DPDVIVDLGL ACLLAGVVGG
RLLHVLADGY FWDYVHLCTD PSLVDWKVEQ ALCEPRYHGV WDAAKGVCHP TERDCLAWAK
FWAGGLTYYG GFVGASAMAY WLLKRDRFPF WKAADMAGFA VPLGLGFGRM GCLLAGCCFG
QRTDGALGLS FPPNSPASEA QFKLHELASA RLPSHPVHPT QIYESAMSFA IAAICLLYVH
GRKRYDGQVF ATFLGLYALG RFTLEFARAD DRGGLIGLST SQLIGVAVIG AAIAIHVARS
RKAAPAAIAP AA
//
