LGT_STRMU
ID LGT_STRMU Reviewed; 259 AA.
AC P72482;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 119.
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=SMU_755;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5 / Kuramitsu;
RA Meloni M., Piggot P.J., Daneo-Moore L.;
RT "Nucleotide sequence of the Streptococcus mutans ptsK and lgt genes.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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, ECO:0000305}.
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DR EMBL; U75480; AAC80171.3; -; Genomic_DNA.
DR EMBL; AE014133; AAN58478.1; -; Genomic_DNA.
DR RefSeq; NP_721172.1; NC_004350.2.
DR RefSeq; WP_002263626.1; NC_004350.2.
DR AlphaFoldDB; P72482; -.
DR SMR; P72482; -.
DR STRING; 210007.SMU_755; -.
DR PRIDE; P72482; -.
DR EnsemblBacteria; AAN58478; AAN58478; SMU_755.
DR KEGG; smu:SMU_755; -.
DR PATRIC; fig|210007.7.peg.668; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_0_1_9; -.
DR OMA; TDVPWAI; -.
DR PhylomeDB; P72482; -.
DR BRENDA; 2.5.1.145; 14748.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000002512; 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..259
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172687"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 114..133
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 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 227..247
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"
FT CONFLICT 13
FT /note="A -> T (in Ref. 1; AAC80171)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="T -> A (in Ref. 1; AAC80171)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="A -> T (in Ref. 1; AAC80171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29850 MW; 56FEBF441E78250A CRC64;
MINPIAIKLG PLAIRWYSIC IVTGLILAVY LTIREAPKKN IKSDDVLDFI LIAFPLAIVG
ARLYYVIFDW DYYLKNPSEI PVIWHGGIAI YGGLLTGALV LFIFSYYRMI KPIDFLDVAT
PGVMLAQSIG RWGNFVNQEA YGKAVTQLNY LPDFIRKQMY IDGHYRTPTF LYESLWNLLG
FIIIMILRRR PNLLKEGEVA FFYLIWYGSG RFVIEGMRTD SLMFASLRVS QWLSVLLVVV
GVILIVIRRR NHAIPYYQC
