ID   LGT_GEOKA               Reviewed;         270 AA.
AC   Q5KVC0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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}; OrderedLocusNames=GK3081;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD77366.1; -; Genomic_DNA.
DR   RefSeq; WP_011232551.1; NC_006510.1.
DR   AlphaFoldDB; Q5KVC0; -.
DR   SMR; Q5KVC0; -.
DR   STRING; 235909.GK3081; -.
DR   EnsemblBacteria; BAD77366; BAD77366; GK3081.
DR   KEGG; gka:GK3081; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_2_9; -.
DR   OMA; FRLNPLW; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001172; Chromosome.
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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..270
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_0000172605"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         137
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   270 AA;  30850 MW;  6F24B1FADBA564A4 CRC64;
     MESTIQPLDR VFLHLGPITI YWYGVIIGTG VLIGLWLATR EAVRRGLPKE TFVDLVLFAV
     PIAIVCARAY YVLFEWHYYS KHLSEIPKVW QGGLAIHGGL IGAVATGAVF ARARGLSFWK
     LADIAAPSII LGQAIGRWGN FMNQEAHGGP VSRQFLENLH LPDWIINQMY IDGRYWHPTF
     LYESLWNLVG FFLLLWLRRV NLRRGELFLS YLIWYSVGRF WIEGMRTDSL MLAGSLRAAQ
     VVSVTLIVLS IALWIVRRAK GWAKARYQDE