LGT_STAXY
ID LGT_STAXY Reviewed; 278 AA.
AC Q9S1H4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=10714994; DOI=10.1128/jb.182.7.1895-1902.2000;
RA Huynh P.L., Jankovic I., Schnell N., Brueckner R.;
RT "Characterization of an HPr kinase mutant of Staphylococcus xylosus.";
RL J. Bacteriol. 182:1895-1902(2000).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01147};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
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DR EMBL; AJ243915; CAB51945.1; -; Genomic_DNA.
DR RefSeq; WP_029377666.1; NZ_VBTJ01000001.1.
DR AlphaFoldDB; Q9S1H4; -.
DR SMR; Q9S1H4; -.
DR STRING; 1288.SXYLSMQ121_1935; -.
DR GeneID; 45497583; -.
DR eggNOG; COG0682; Bacteria.
DR OrthoDB; 435911at2; -.
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 membrane; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..278
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172681"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01147"
SQ SEQUENCE 278 AA; 31764 MW; 2AC5CD51EFC593A2 CRC64;
MLTLNYIDPI AFELGPISVR WYGIIIAAGI LLGYFIAQAS VKKIGYDQDT LVDIIFWSAI
FGFIVARIYF VIFQWPYYIQ NPIEIPMIWH GGIAIHGGLI GGFVTGIIIC KQKNINPFQI
GDVIAPSMIL GQGIGRWGNF MNHEAHGGPI SRSVLENLHI PNFIIDNMYI DGKYYQPTFL
YESLWDILGF VILILLRKHL RVGDTFCLYL IWYSIGRFFV EGMRTDSLML TSDIRVAQLM
SIILILIGVI IMIIRRVKYR SPRYKDVGPL SWPNPKVK
