ID   LGT_CLOD6               Reviewed;         248 AA.
AC   Q182Z4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=CD630_26590;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ69545.1; -; Genomic_DNA.
DR   RefSeq; WP_009897834.1; NZ_CP010905.2.
DR   RefSeq; YP_001089170.1; NC_009089.1.
DR   AlphaFoldDB; Q182Z4; -.
DR   SMR; Q182Z4; -.
DR   STRING; 272563.CD630_26590; -.
DR   EnsemblBacteria; CAJ69545; CAJ69545; CD630_26590.
DR   GeneID; 66355061; -.
DR   KEGG; cdf:CD630_26590; -.
DR   KEGG; pdc:CDIF630_02913; -.
DR   PATRIC; fig|272563.120.peg.2802; -.
DR   eggNOG; COG0682; Bacteria.
DR   OMA; TDVPWAI; -.
DR   PhylomeDB; Q182Z4; -.
DR   BioCyc; PDIF272563:G12WB-2810-MON; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001978; 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..248
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_1000053418"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         130
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   248 AA;  27538 MW;  4E37094C1B6CD91D CRC64;
     MDRVAFTLFG IDIMWYGILM ACGMILGTLI AIKEAKRVGI KEDDVLNIAI IAIPVGLICA
     RIYYVVFNWS YYAQNMSQIF NFRGGGLAIH GGLIGGILAG YIYTKIKNIN FLKMADTVIL
     GMPLAQAIGR WGNFINGEAH GGATNLPWGI MVDGVKVHPT FLYESIWDFG IFIVLLLFRK
     NKKYEGQVIV TYITLYSIGR FFIEGLRTDS LMLGPLRMAQ VISLIGVIGG IIAHVYLSKK
     NKNNISEE