ID   LGT_CUPPJ               Reviewed;         276 AA.
AC   Q475B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Reut_A0641;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ60023.1; -; Genomic_DNA.
DR   RefSeq; WP_011296828.1; NC_007347.1.
DR   AlphaFoldDB; Q475B0; -.
DR   SMR; Q475B0; -.
DR   STRING; 264198.Reut_A0641; -.
DR   EnsemblBacteria; AAZ60023; AAZ60023; Reut_A0641.
DR   KEGG; reu:Reut_A0641; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_0_4; -.
DR   OMA; TDVPWAI; -.
DR   OrthoDB; 435911at2; -.
DR   UniPathway; UPA00664; -.
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..276
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_1000053484"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         142
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   276 AA;  31193 MW;  124AF3B5486281ED CRC64;
     MLIHPQFDPV AIHIGPLAIR WYGLMYLAGF IMFLWFGRLR IRQPHMAARG WAARDLDDML
     FFGVMGVILG GRLGYVLFYK PSYYLTHPLE IFKVWEGGMA FHGGFLGVLV AMWLFARLRQ
     RHWLEVTDFI APMIPCGLAA GRIGNFINGE LWGRPTDLPW GMIFPQAGDN IPRHPSQLYQ
     FAGEGVALFI ILWLFARKPR PMGAVSGVFL IGYGGFRFAA EFAREPDSFL GLLAMHLSMG
     QWLSLPMILI GIAMVVWAYR RQARSGEERP VTDSGA