U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

lpxT lipid A-core phosphotransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946693, updated on 2-May-2024

Summary

Go to the top of the page Help
Gene symbol
lpxT
Gene description
lipid A-core phosphotransferase
Primary source
ASAP:ABE-0007196
Locus tag
b2174
See related
ECOCYC:G7146
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2168; yeiU
Summary
One third of the lipid A pool is lipid A 1-diphosphate formed by a periplasmic domain of LpxT (Touze, 2008). ybjG, pgpB, and lpxT are paralogs. [More information is available at EcoGene: EG14075]. LpxT is responsible for transfer of a phosphate group from undecaprenyl-pyrophosphate to the position 1 phosphate of approximately one-third of lipid A molecules to create lipid A 1-diphosphate. [More information is available at EcoCyc: G7146].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (2268854..2269567)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative oxidoreductase YeiQ Neighboring gene zinc-binding GTPase YeiR Neighboring gene peptidoglycan endopeptidase/peptidoglycan L,D-carboxypeptidase Neighboring gene putative c-di-GMP phosphodiesterase PdeN

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Temperature-dependent regulation of the Escherichia coli lpxT gene. Sciandrone B, et al. Biochim Biophys Acta Gene Regul Mech, 2019 Aug. PMID 31299227
  2. LpxT-Dependent Phosphorylation of Lipid A in Escherichia coli Increases Resistance to Deoxycholate and Enhances Gut Colonization. Tian X, et al. Front Microbiol, 2021. PMID 34017319, Free PMC Article
  3. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Herrera CM, et al. Mol Microbiol, 2010 Jun. PMID 20384697, Free PMC Article
  4. Undecaprenyl phosphate recycling comes out of age. Valvano MA. Mol Microbiol, 2008 Jan. PMID 18086187
  5. Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. Pomposiello PJ, et al. J Bacteriol, 2001 Jul. PMID 11395452, Free PMC Article

See all (18) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Results show that the Escherichia coli lpxT gene is down-regulated upon temperature upshift and found that the protein stability is not affected by the temperature change. Conversely, the lpxT mRNA levels strongly decrease upon a shift from 28 to 42 degrees C. The lpxT promoter has a temperature-sensitive activity depending on its peculiar -10 region.
    Title: Temperature-dependent regulation of the Escherichia coli lpxT gene.
  2. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is shown here to be critical for Escherichia coli to resist the bactericidal activity of polymyxin.
    Title: Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides.
  3. Together, the results support the notion that YbjG, and to a lesser extent YeiU, exert their enzymic activity on the periplasmic side of the plasma membrane and are implicated in the recycling of periplasmic undecaprenyl pyrophosphate molecules.
    Title: An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling.
Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables phosphotransferase activity, phosphate group as acceptor IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphotransferase activity, phosphate group as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
enables undecaprenyl-diphosphatase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in Gram-negative-bacterium-type cell outer membrane assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid A biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipopolysaccharide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in response to bile acid IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
lipid A-core phosphotransferase
NP_416679.4

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    2268854..2269567
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416679.4 lipid A-core phosphotransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416679.4

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376SBR1, A0A418GGF0, A0A8S7HXC4, A0AA87KP67
    Conserved Domains (1) summary
    smart00014
    Location:98 → 210
    acidPPc; Acid phosphatase homologues
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.