LGT_AZOBR
ID LGT_AZOBR Reviewed; 268 AA.
AC Q8KSV0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147};
DE EC=2.5.1.145 {ECO:0000255|HAMAP-Rule:MF_01147};
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen S.F., Sun W.G., Li J.L.;
RT "Cloning and sequencing of several ORFs from Azospirillum brasilense.";
RL Submitted (APR-2002) 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:0000255|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:0000255|HAMAP-Rule:MF_01147};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
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DR EMBL; AF510422; AAM53572.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KSV0; -.
DR SMR; Q8KSV0; -.
DR UniPathway; UPA00664; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; PTHR30589; 1.
DR Pfam; PF01790; LGT; 1.
DR TIGRFAMs; TIGR00544; lgt; 1.
DR PROSITE; PS01311; LGT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..268
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172544"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT BINDING 141
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
SQ SEQUENCE 268 AA; 29301 MW; D04530E78E99EAC7 CRC64;
MLAIAFPGID PVAFELGPIV IRWYALAYLA GFVLGWRYCL ALARSTPGRP SAEDYDDFLT
WAVVGVILGG RIGYVLFYNL PFYLQNPLDA LMVWHGGMSF HGGLIGVLGA ILLFCWKRGL
SPLAFGDLIA AAAPIGLFFG RIANFINGEL YGRPAPDVSW AVVFPRDPLQ VPRHPSQLYE
SFLEGAVLFV LLAILVRMPA VRGRAGMTAG IFFIGYGLSR IIAEFFREPD AQLGFLYAGA
TMGQLLSVPM VLFGVWLVAQ ARRRPAAI