ID   LGT_NITEU               Reviewed;         278 AA.
AC   Q820A4;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=NE0105;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84016.1; -; Genomic_DNA.
DR   RefSeq; WP_011110757.1; NC_004757.1.
DR   AlphaFoldDB; Q820A4; -.
DR   SMR; Q820A4; -.
DR   STRING; 228410.NE0105; -.
DR   EnsemblBacteria; CAD84016; CAD84016; NE0105.
DR   KEGG; neu:NE0105; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_0_4; -.
DR   OMA; TDVPWAI; -.
DR   OrthoDB; 435911at2; -.
DR   PhylomeDB; Q820A4; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001416; 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..278
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_0000172642"
FT   TRANSMEM        17..37
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        89..109
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        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        233..253
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   278 AA;  31308 MW;  7D330E8F53779576 CRC64;
     MLVHPQFDPV AISIGPLAVR WYGLMYLLGF SLFILLGRYR IRQQPNGVFT REMLDDALFY
     GVLGVILGGR LGHVLFYEPG YYLQHPLEIL AIWQGGMSFH GGFLGVAIAM LCLARKYQLS
     WLAVTDFIAP LVPLGLGAGR IGNFINGELW GRPTDVPWGM IFPYADNLPR HPSQLYEFAL
     EGLVLFALIW LYSAKPRPLG AVTGMFMIGY GAFRSFCEFF REPDDGFLGI MTLGISMGQW
     LSLPMIAAGI ALLYWAYRYD GKPEKAARKL PRERKNRD