LGT_ECOLI
ID LGT_ECOLI Reviewed; 291 AA.
AC P60955; P37149; Q2MA09;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000303|PubMed:7896715};
DE EC=2.5.1.145 {ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000269|PubMed:26729647, ECO:0000269|PubMed:7896715, ECO:0000269|PubMed:8051048};
DE AltName: Full=Prolipoprotein diacylglyceryl transferase {ECO:0000305};
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000303|PubMed:7896715};
GN Synonyms=umpA {ECO:0000303|PubMed:7896715};
GN OrderedLocusNames=b2828 {ECO:0000312|EMBL:AAC75867.1},
GN JW2796 {ECO:0000312|EMBL:BAE76897.1};
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=7896715; DOI=10.1128/jb.177.7.1879-1882.1995;
RA Gan K., Sankaran K., Williams M.G., Aldea M., Rudd K.E., Kushner S.R.,
RA Wu H.C.;
RT "The umpA gene of Escherichia coli encodes
RT phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and
RT regulates thymidylate synthase levels through translational coupling.";
RL J. Bacteriol. 177:1879-1882(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-291.
RC STRAIN=K12 / JM103 / ATCC 39403 / DSM 2829 / KCTC 1112 / NCIMB 12044;
RX PubMed=6308660; DOI=10.1073/pnas.80.16.4914;
RA Belfort M., Maley G.F., Pedersen-Lane J., Maley F.;
RT "Primary structure of the Escherichia coli thyA gene and its thymidylate
RT synthase product.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4914-4918(1983).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8051048; DOI=10.1016/s0021-9258(17)32077-x;
RA Sankaran K., Wu H.C.;
RT "Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl
RT moiety from phosphatidylglycerol.";
RL J. Biol. Chem. 269:19701-19706(1994).
RN [6]
RP VARIANTS SK634; SK635 AND SK636.
RX PubMed=7592473; DOI=10.1128/jb.177.23.6820-6824.1995;
RA Qi H.Y., Sankaran K., Gan K., Wu H.C.;
RT "Structure-function relationship of bacterial prolipoprotein diacylglyceryl
RT transferase: functionally significant conserved regions.";
RL J. Bacteriol. 177:6820-6824(1995).
RN [7]
RP MUTAGENESIS OF HIS-7; HIS-24; TYR-26; TYR-62; TYR-76; HIS-103; TYR-190;
RP HIS-196; TYR-201; TYR-235; TYR-282 AND HIS-289.
RX PubMed=9139912; DOI=10.1128/jb.179.9.2944-2948.1997;
RA Sankaran K., Gan K., Rash B., Qi H.-Y., Wu H.C., Rick P.D.;
RT "Roles of histidine-103 and tyrosine-235 in the function of the
RT prolipoprotein diacylglyceryl transferase of Escherichia coli.";
RL J. Bacteriol. 179:2944-2948(1997).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP TYR-26; GLY-98; HIS-103; GLY-104; ASP-129; ARG-143; ASN-146; GLU-151;
RP GLY-154; ARG-239 AND GLU-243.
RX PubMed=22287519; DOI=10.1128/jb.06641-11;
RA Pailler J., Aucher W., Pires M., Buddelmeijer N.;
RT "Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of
RT Escherichia coli has seven transmembrane segments, and its essential
RT residues are embedded in the membrane.";
RL J. Bacteriol. 194:2142-2151(2012).
RN [10] {ECO:0007744|PDB:5AZB, ECO:0007744|PDB:5AZC}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH
RP PHOSPHATIDYLGLYCEROL AND PALMITATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND
RP MUTAGENESIS OF ARG-143.
RX PubMed=26729647; DOI=10.1038/ncomms10198;
RA Mao G., Zhao Y., Kang X., Li Z., Zhang Y., Wang X., Sun F., Sankaran K.,
RA Zhang X.C.;
RT "Crystal structure of E. coli lipoprotein diacylglyceryl transferase.";
RL Nat. Commun. 7:10198-10198(2016).
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 ECO:0000269|PubMed:26729647, ECO:0000269|PubMed:7896715,
CC ECO:0000269|PubMed:8051048}.
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 ECO:0000269|PubMed:26729647, ECO:0000269|PubMed:7896715,
CC ECO:0000269|PubMed:8051048};
CC -!- ACTIVITY REGULATION: Inhibited by palmitate.
CC {ECO:0000269|PubMed:26729647}.
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000269|PubMed:26729647, ECO:0000269|PubMed:7896715,
CC ECO:0000269|PubMed:8051048}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01147, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:22287519, ECO:0000269|PubMed:26729647}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000269|PubMed:22287519, ECO:0000269|PubMed:26729647}.
CC -!- DOMAIN: Contains several lipid molecules that are bound within the
CC central cavity of the protein. {ECO:0000269|PubMed:26729647}.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in diacylglyceryl
CC modification of prolipoprotein. {ECO:0000269|PubMed:22287519,
CC ECO:0000269|PubMed:7896715}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12289; AAA69024.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40475.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75867.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76897.1; -; Genomic_DNA.
DR EMBL; J01710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A56149; A56149.
DR RefSeq; NP_417305.1; NC_000913.3.
DR RefSeq; WP_000204658.1; NZ_STEB01000034.1.
DR PDB; 5AZB; X-ray; 1.60 A; A=2-291.
DR PDB; 5AZC; X-ray; 1.90 A; A=2-291.
DR PDBsum; 5AZB; -.
DR PDBsum; 5AZC; -.
DR AlphaFoldDB; P60955; -.
DR SMR; P60955; -.
DR BioGRID; 4263276; 176.
DR STRING; 511145.b2828; -.
DR ChEMBL; CHEMBL3309026; -.
DR jPOST; P60955; -.
DR PaxDb; P60955; -.
DR PRIDE; P60955; -.
DR EnsemblBacteria; AAC75867; AAC75867; b2828.
DR EnsemblBacteria; BAE76897; BAE76897; BAE76897.
DR GeneID; 66673305; -.
DR GeneID; 947303; -.
DR KEGG; ecj:JW2796; -.
DR KEGG; eco:b2828; -.
DR PATRIC; fig|1411691.4.peg.3907; -.
DR EchoBASE; EB2049; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_6; -.
DR InParanoid; P60955; -.
DR OMA; TDVPWAI; -.
DR PhylomeDB; P60955; -.
DR BioCyc; EcoCyc:EG12128-MON; -.
DR BioCyc; MetaCyc:EG12128-MON; -.
DR BRENDA; 2.5.1.145; 2026.
DR UniPathway; UPA00664; -.
DR PRO; PR:P60955; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IDA:EcoCyc.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172596"
FT TOPO_DOM 1..24
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22287519,
FT ECO:0000269|PubMed:26729647"
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 44..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 77..98
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 120..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 151..197
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 219..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 245..261
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:22287519"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000312|PDB:5AZB"
FT TOPO_DOM 283..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26729647,
FT ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:22287519"
FT BINDING 143
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,
FT ECO:0000269|PubMed:26729647"
FT VARIANT 25
FT /note="W -> R (in SK636, temperature-sensitive)"
FT /evidence="ECO:0000305|PubMed:7592473"
FT VARIANT 104
FT /note="G -> S (in SK634, temperature-sensitive)"
FT /evidence="ECO:0000305|PubMed:7592473"
FT VARIANT 139
FT /note="L -> F (in SK635, temperature-sensitive)"
FT /evidence="ECO:0000305|PubMed:7592473"
FT MUTAGEN 7
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 24
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 26
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 26
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 62
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 76
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 98
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 103
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 103
FT /note="H->Q: Loss of activity (PubMed:9139912). No effect
FT (PubMed:22287519)."
FT /evidence="ECO:0000269|PubMed:22287519,
FT ECO:0000269|PubMed:9139912"
FT MUTAGEN 104
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 129
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 143
FT /note="R->A: Decrease in activity. No effect on affinity
FT for lipids."
FT /evidence="ECO:0000269|PubMed:22287519,
FT ECO:0000269|PubMed:26729647"
FT MUTAGEN 146
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 151
FT /note="E->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 154
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 190
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 196
FT /note="H->N,L: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 196
FT /note="H->Q,R: 50% decrease in activity."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 201
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 235
FT /note="Y->F,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 235
FT /note="Y->S: 37% decrease in activity."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 239
FT /note="R->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 243
FT /note="E->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:22287519"
FT MUTAGEN 282
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT MUTAGEN 289
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:9139912"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5AZB"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:5AZB"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 54..80
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:5AZB"
FT HELIX 255..284
FT /evidence="ECO:0007829|PDB:5AZB"
SQ SEQUENCE 291 AA; 33108 MW; 5F946E4E60D0112A CRC64;
MTSSYLHFPE FDPVIFSIGP VALHWYGLMY LVGFIFAMWL ATRRANRPGS GWTKNEVENL
LYAGFLGVFL GGRIGYVLFY NFPQFMADPL YLFRVWDGGM SFHGGLIGVI VVMIIFARRT
KRSFFQVSDF IAPLIPFGLG AGRLGNFING ELWGRVDPNF PFAMLFPGSR TEDILLLQTN
PQWQSIFDTY GVLPRHPSQL YELLLEGVVL FIILNLYIRK PRPMGAVSGL FLIGYGAFRI
IVEFFRQPDA QFTGAWVQYI SMGQILSIPM IVAGVIMMVW AYRRSPQQHV S
