ID   LGT_XANOP               Reviewed;         296 AA.
AC   B2SPS7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=PXO_04650;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(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 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; CP000967; ACD57764.1; -; Genomic_DNA.
DR   RefSeq; WP_011260173.1; NC_010717.2.
DR   AlphaFoldDB; B2SPS7; -.
DR   SMR; B2SPS7; -.
DR   STRING; 360094.PXO_04650; -.
DR   EnsemblBacteria; ACD57764; ACD57764; PXO_04650.
DR   KEGG; xop:PXO_04650; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_0_6; -.
DR   OMA; TDVPWAI; -.
DR   OrthoDB; 435911at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001740; 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..296
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_1000137473"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        57..77
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        119..139
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        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         140
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   296 AA;  32670 MW;  6D3EEE522BF72DE1 CRC64;
     MIYLHAIDPI AFSLGPVKVH WYGLMYLAAF FSAWSLGRSR ILRGRLPGVD MDGFSDLLFY
     GMLGVVLGGR IGYMLFYAFE TFVANPLILF KVWEGGMSFH GGLLGVLVAC WLWARKHRLH
     FFDVMDFVAP LVPLGLGFGR LGNFVGGELW GKFTQAGWGV IFPHAPELAD QLPAQIQAQY
     AAGALNQLAR HPSQLYEAAL EGVVMFVVLW TFSMKPRARY ALSGLFALLY GVFRFIVEFV
     RVPDAPIGYL AFNWLTMGQI LSLPLIAVGL ALLAMSRRAP VLQPVLPTPA GVEAAK