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LGT_PSE14
ID   LGT_PSE14               Reviewed;         270 AA.
AC   Q48CC8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=PSPPH_4873;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35179.1; -; Genomic_DNA.
DR   RefSeq; WP_004655000.1; NC_005773.3.
DR   AlphaFoldDB; Q48CC8; -.
DR   SMR; Q48CC8; -.
DR   STRING; 264730.PSPPH_4873; -.
DR   EnsemblBacteria; AAZ35179; AAZ35179; PSPPH_4873.
DR   GeneID; 61872409; -.
DR   KEGG; psp:PSPPH_4873; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_1_0_6; -.
DR   OMA; TDVPWAI; -.
DR   OrthoDB; 435911at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000000551; 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..270
FT                   /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT                   transferase"
FT                   /id="PRO_1000053473"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        56..76
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        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT   TRANSMEM        175..195
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         139
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   270 AA;  30115 MW;  9317F2BD45CE9E00 CRC64;
     MLPYPQIDPV AVAIGPLQIH WYGLMYLVGI GGAWLLASRR LNKFDPTWTK EKLSDLIFWL
     AMGVIVGGRL GYVLFYDLSA YIANPLLIFE VWKGGMAFHG GFVGVMIAAW WFGKRNGKSF
     FQLMDFVAPL VPIGLGAGRI GNFINAELWG KPTDVPWAMV FPPFSDPAQL ARHPSQLYQF
     ALEGVALFII LNLYARKPRP TMAVSGMFAL FYGIFRFVVE FVRVPDAQLG YLAWGWVTMG
     QILSLPMIIA GLFLIWLAYK RDPAASKAAA
 
 
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