ID   LGT_RUEPO               Reviewed;         295 AA.
AC   Q5LUZ4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=SPO0908;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV94213.1; -; Genomic_DNA.
DR   RefSeq; WP_011046657.1; NC_003911.12.
DR   AlphaFoldDB; Q5LUZ4; -.
DR   SMR; Q5LUZ4; -.
DR   STRING; 246200.SPO0908; -.
DR   EnsemblBacteria; AAV94213; AAV94213; SPO0908.
DR   KEGG; sil:SPO0908; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_0_5; -.
DR   OMA; TDVPWAI; -.
DR   OrthoDB; 435911at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001023; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..295
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_0000172671"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   BINDING         152
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   295 AA;  32266 MW;  C518A41F405BB06C CRC64;
     MQAVLNFPDL SPELFSISLF GMEFALRWYA LAYIAGIVIA WRLAVLATRR AALWPANTPP
     MAPARIEDLL TWIILGVILG GRLGFVLFYQ PAYYLANPTE ILMVWQGGMA FHGGLLGVVI
     AAWLYSLRHN IPKLSLADLI THTVAPGLLL GRLANFINAE LWGRPSDLPW AVIFPGPAAQ
     ACPGVVGLCA RHPSQLYEAA LEGLLLGTLL LWLVWRRGAL KRPGLITGVF LAGYGLSRFV
     VEFFRQPDAQ FVTPGNPLGL AWQVGEYGLT MGQLLSLPMI ALGLWFVLRA RAVPA