ID   LGT_STRPZ               Reviewed;         259 AA.
AC   B5XKG1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Spy49_0495;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
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; CP000829; ACI60823.1; -; Genomic_DNA.
DR   RefSeq; WP_002990577.1; NC_011375.1.
DR   AlphaFoldDB; B5XKG1; -.
DR   SMR; B5XKG1; -.
DR   EnsemblBacteria; ACI60823; ACI60823; Spy49_0495.
DR   KEGG; soz:Spy49_0495; -.
DR   HOGENOM; CLU_013386_0_1_9; -.
DR   OMA; TDVPWAI; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001039; 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; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..259
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_1000137466"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         131
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   259 AA;  29420 MW;  5854C826BDE51CF6 CRC64;
     MINPIALKCG PLAIHWYALC ILSGLVLAVY LASKEAPKKG ISSDAIFDFI LIAFPLAIVG
     ARIYYVIFEW SYYVKHLDEI IAIWNGGIAI YGGLITGALV LLAYCYNKVL NPIHFLDIAA
     PSVMVAQAIG RWGNFINQEA YGKAVSQLNY LPSFIQKQMF IEGSYRIPTF LYESLWNLLG
     FVIIMMWRRK PKSLLDGEIF AFYLIWYGSG RLVIEGMRTD SLMFLGIRIS QYVSALLIII
     GLIFVIKRRR QKGISYYQE