LGT_METPP
ID LGT_METPP Reviewed; 264 AA.
AC A2SFL2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Mpe_A1389;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM94351.1; -; Genomic_DNA.
DR RefSeq; WP_011828988.1; NC_008825.1.
DR AlphaFoldDB; A2SFL2; -.
DR SMR; A2SFL2; -.
DR STRING; 420662.Mpe_A1389; -.
DR PRIDE; A2SFL2; -.
DR EnsemblBacteria; ABM94351; ABM94351; Mpe_A1389.
DR KEGG; mpt:Mpe_A1389; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_4; -.
DR OMA; TDVPWAI; -.
DR OrthoDB; 435911at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000000366; 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..264
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_1000053453"
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 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 241..261
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 264 AA; 29286 MW; 486474DE6CEDE5B8 CRC64;
MLIHPQFDPV ALELGPLAIH WYGLTYLVAF GLFLWLASLR VQHSPFRETG WTRRDVEDLL
FYGVLGVIIG GRLGYVLFYK PGYYAAHPLE VFEVWKGGMA FHGGLLGVIG AMALFARTRG
RRWLEVTDLI APCVPTGLAS GRIGNFINGE LWGRAADPSL PWAMVYPQSG SEIPRHPSPL
YQFALEGLLL FVVLWLYARK PRATGQVSGA FLVGYGVLRF IAEYFREPDG FLGLLALGMS
MGQWLCVPMV AAGVALWVWA GRRA