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Protein

Prolipoprotein diacylglyceryl transferase

Gene

lgt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins.1 Publication

Pathwayi: lipoprotein biosynthesis (diacylglyceryl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (diacylglyceryl transfer), which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (diacylglyceryl transfer) and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • lipoprotein biosynthetic process Source: EcoCyc
  • protein lipoylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG12128-MONOMER.
ECOL316407:JW2796-MONOMER.
MetaCyc:EG12128-MONOMER.
UniPathwayiUPA00664.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolipoprotein diacylglyceryl transferase (EC:2.4.99.-)
Gene namesi
Name:lgt
Synonyms:umpA
Ordered Locus Names:b2828Imported, JW2796Imported
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12128. lgt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Periplasmic1 PublicationAdd
BLAST
Transmembranei21 – 4121HelicalSequence analysisAdd
BLAST
Topological domaini42 – 5918Cytoplasmic1 PublicationAdd
BLAST
Transmembranei60 – 8021HelicalSequence analysisAdd
BLAST
Topological domaini81 – 9515Periplasmic1 PublicationAdd
BLAST
Transmembranei96 – 11621HelicalSequence analysisAdd
BLAST
Topological domaini117 – 12913Cytoplasmic1 PublicationAdd
BLAST
Transmembranei130 – 15021HelicalSequence analysisAdd
BLAST
Topological domaini151 – 19747Periplasmic1 PublicationAdd
BLAST
Transmembranei198 – 21821HelicalSequence analysisAdd
BLAST
Topological domaini219 – 2246Cytoplasmic1 Publication
Transmembranei225 – 24521HelicalSequence analysisAdd
BLAST
Topological domaini246 – 25914Periplasmic1 PublicationAdd
BLAST
Transmembranei260 – 28021HelicalSequence analysisAdd
BLAST
Topological domaini281 – 29111Cytoplasmic2 PublicationsAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutants are defective in diacylglyceryl modification of prolipoprotein.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71H → Q: No effect. 1 Publication
Mutagenesisi24 – 241H → Q: No effect. 1 Publication
Mutagenesisi26 – 261Y → A: Loss of activity. 1 Publication
Mutagenesisi26 – 261Y → F: No effect. 1 Publication
Mutagenesisi62 – 621Y → F: No effect. 1 Publication
Mutagenesisi76 – 761Y → F: No effect. 1 Publication
Mutagenesisi98 – 981G → A: No effect. 1 Publication
Mutagenesisi103 – 1031H → N: Loss of activity. 1 Publication
Mutagenesisi103 – 1031H → Q: Loss of activity (PubMed:9139912). No effect (PubMed:22287519). 2 Publications
Mutagenesisi104 – 1041G → A: No effect. 1 Publication
Mutagenesisi129 – 1291D → A: No effect. 1 Publication
Mutagenesisi143 – 1431R → A: Decrease in activity. 1 Publication
Mutagenesisi146 – 1461N → A: Loss of activity. 1 Publication
Mutagenesisi151 – 1511E → A: Decrease in activity. 1 Publication
Mutagenesisi154 – 1541G → A: Loss of activity. 1 Publication
Mutagenesisi190 – 1901Y → F: No effect. 1 Publication
Mutagenesisi196 – 1961H → N or L: No effect. 1 Publication
Mutagenesisi196 – 1961H → Q or R: 50% decrease in activity. 1 Publication
Mutagenesisi201 – 2011Y → F: No effect. 1 Publication
Mutagenesisi235 – 2351Y → F or T: Loss of activity. 1 Publication
Mutagenesisi235 – 2351Y → S: 37% decrease in activity. 1 Publication
Mutagenesisi239 – 2391R → A: Decrease in activity. 1 Publication
Mutagenesisi243 – 2431E → A: Decrease in activity. 1 Publication
Mutagenesisi282 – 2821Y → F: No effect. 1 Publication
Mutagenesisi289 – 2891H → Q: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Prolipoprotein diacylglyceryl transferasePRO_0000172596Add
BLAST

Proteomic databases

PaxDbiP60955.

Interactioni

Protein-protein interaction databases

BioGridi4263276. 97 interactions.
STRINGi511145.b2828.

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi13 – 186Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 4521Combined sources
Helixi54 – 8027Combined sources
Helixi82 – 876Combined sources
Helixi89 – 935Combined sources
Helixi95 – 973Combined sources
Helixi102 – 11918Combined sources
Helixi124 – 1318Combined sources
Helixi132 – 1343Combined sources
Helixi135 – 14814Combined sources
Helixi167 – 1693Combined sources
Helixi170 – 1778Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 1907Combined sources
Helixi198 – 2069Combined sources
Helixi208 – 21710Combined sources
Helixi226 – 24318Combined sources
Helixi255 – 28430Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AZBX-ray1.60A2-291[»]
5AZCX-ray1.90A2-291[»]
ProteinModelPortaliP60955.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Lgt family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C3B. Bacteria.
COG0682. LUCA.
HOGENOMiHOG000098666.
InParanoidiP60955.
KOiK13292.
OMAiAHRTKRH.
OrthoDBiEOG6MH5CQ.
PhylomeDBiP60955.

Family and domain databases

HAMAPiMF_01147. Lgt.
InterProiIPR001640. Prolipoprot_diAcglycer_Trfase.
[Graphical view]
PfamiPF01790. LGT. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00544. lgt. 1 hit.
PROSITEiPS01311. LGT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60955-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSYLHFPE FDPVIFSIGP VALHWYGLMY LVGFIFAMWL ATRRANRPGS
60 70 80 90 100
GWTKNEVENL LYAGFLGVFL GGRIGYVLFY NFPQFMADPL YLFRVWDGGM
110 120 130 140 150
SFHGGLIGVI VVMIIFARRT KRSFFQVSDF IAPLIPFGLG AGRLGNFING
160 170 180 190 200
ELWGRVDPNF PFAMLFPGSR TEDILLLQTN PQWQSIFDTY GVLPRHPSQL
210 220 230 240 250
YELLLEGVVL FIILNLYIRK PRPMGAVSGL FLIGYGAFRI IVEFFRQPDA
260 270 280 290
QFTGAWVQYI SMGQILSIPM IVAGVIMMVW AYRRSPQQHV S
Length:291
Mass (Da):33,108
Last modified:April 26, 2004 - v1
Checksum:i5F946E4E60D0112A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251W → R in SK636, temperature-sensitive.
Natural varianti104 – 1041G → S in SK634, temperature-sensitive.
Natural varianti139 – 1391L → F in SK635, temperature-sensitive.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12289 Genomic DNA. Translation: AAA69024.1.
U29581 Genomic DNA. Translation: AAB40475.1.
U00096 Genomic DNA. Translation: AAC75867.1.
AP009048 Genomic DNA. Translation: BAE76897.1.
J01710 Genomic DNA. No translation available.
PIRiA56149.
RefSeqiNP_417305.1. NC_000913.3.
WP_000204658.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75867; AAC75867; b2828.
BAE76897; BAE76897; BAE76897.
GeneIDi947303.
KEGGiecj:JW2796.
eco:b2828.
PATRICi32121074. VBIEscCol129921_2926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12289 Genomic DNA. Translation: AAA69024.1.
U29581 Genomic DNA. Translation: AAB40475.1.
U00096 Genomic DNA. Translation: AAC75867.1.
AP009048 Genomic DNA. Translation: BAE76897.1.
J01710 Genomic DNA. No translation available.
PIRiA56149.
RefSeqiNP_417305.1. NC_000913.3.
WP_000204658.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AZBX-ray1.60A2-291[»]
5AZCX-ray1.90A2-291[»]
ProteinModelPortaliP60955.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263276. 97 interactions.
STRINGi511145.b2828.

Proteomic databases

PaxDbiP60955.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75867; AAC75867; b2828.
BAE76897; BAE76897; BAE76897.
GeneIDi947303.
KEGGiecj:JW2796.
eco:b2828.
PATRICi32121074. VBIEscCol129921_2926.

Organism-specific databases

EchoBASEiEB2049.
EcoGeneiEG12128. lgt.

Phylogenomic databases

eggNOGiENOG4105C3B. Bacteria.
COG0682. LUCA.
HOGENOMiHOG000098666.
InParanoidiP60955.
KOiK13292.
OMAiAHRTKRH.
OrthoDBiEOG6MH5CQ.
PhylomeDBiP60955.

Enzyme and pathway databases

UniPathwayiUPA00664.
BioCyciEcoCyc:EG12128-MONOMER.
ECOL316407:JW2796-MONOMER.
MetaCyc:EG12128-MONOMER.

Miscellaneous databases

PROiP60955.

Family and domain databases

HAMAPiMF_01147. Lgt.
InterProiIPR001640. Prolipoprot_diAcglycer_Trfase.
[Graphical view]
PfamiPF01790. LGT. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00544. lgt. 1 hit.
PROSITEiPS01311. LGT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling."
    Gan K., Sankaran K., Williams M.G., Aldea M., Rudd K.E., Kushner S.R., Wu H.C.
    J. Bacteriol. 177:1879-1882(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, DISRUPTION PHENOTYPE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product."
    Belfort M., Maley G.F., Pedersen-Lane J., Maley F.
    Proc. Natl. Acad. Sci. U.S.A. 80:4914-4918(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-291.
    Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044.
  5. "Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol."
    Sankaran K., Wu H.C.
    J. Biol. Chem. 269:19701-19706(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  6. "Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions."
    Qi H.Y., Sankaran K., Gan K., Wu H.C.
    J. Bacteriol. 177:6820-6824(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SK634; SK635 AND SK636.
  7. "Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli."
    Sankaran K., Gan K., Rash B., Qi H.-Y., Wu H.C., Rick P.D.
    J. Bacteriol. 179:2944-2948(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-7; HIS-24; TYR-26; TYR-62; TYR-76; HIS-103; TYR-190; HIS-196; TYR-201; TYR-235; TYR-282 AND HIS-289.
  8. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane."
    Pailler J., Aucher W., Pires M., Buddelmeijer N.
    J. Bacteriol. 194:2142-2151(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE, MUTAGENESIS OF TYR-26; GLY-98; HIS-103; GLY-104; ASP-129; ARG-143; ASN-146; GLU-151; GLY-154; ARG-239 AND GLU-243.

Entry informationi

Entry nameiLGT_ECOLI
AccessioniPrimary (citable) accession number: P60955
Secondary accession number(s): P37149, Q2MA09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 13, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.