LGT_RICTY
ID LGT_RICTY Reviewed; 259 AA.
AC Q68XS2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=RT0084;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
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DR EMBL; AE017197; AAU03570.1; -; Genomic_DNA.
DR RefSeq; WP_011190557.1; NC_006142.1.
DR AlphaFoldDB; Q68XS2; -.
DR SMR; Q68XS2; -.
DR STRING; 257363.RT0084; -.
DR EnsemblBacteria; AAU03570; AAU03570; RT0084.
DR KEGG; rty:RT0084; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_5; -.
DR OMA; TDVPWAI; -.
DR OrthoDB; 435911at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000000604; 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 inner membrane; Cell membrane; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..259
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172665"
FT TRANSMEM 9..29
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 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT BINDING 138
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; 29438 MW; F73D6401EFD8EE31 CRC64;
MILPNINPII FSIGPFSISW YSLSYVVGIL LGWFYATKII EKFKPEITKK HIEDFITYAI
IGIIVGGRLG YVLLYNPLKY FANPIEILKT YEGGMSFHGA TIGIIISAYL FCQKYKINFL
SLTDIITTVV PIGLFLGRIA NFINCELYGR ITNSSFGIIF PNSDLEPRHP SQLYEAFFEG
LILFCILAYA VFRHDTLKKQ GLNSGIYLIF YSLFRIIIEM FREPDIQIGF ILDSLTMGQI
LSAPMLLLGS YLICRLNSK
