P76445 · LPXT_ECOLI

Function

function

Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P) (PubMed:18047581).
In vitro, has low undecaprenyl-diphosphate phosphatase activity (PubMed:17660416).

Miscellaneous

In E.coli, lipid A contains typically a monophosphate unit at positions 1 and 4' (bis-phosphorylated lipid A). However, one-third of the lipid A contains an unsubstituted diphosphate unit at position 1 (lipid A 1-diphosphate).

Catalytic activity

Activity regulation

Inhibited by BasR. This regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane.

pH Dependence

Optimum pH is 7.0. Significant activity is observed from pH 5.5 to pH 7.5.

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionphosphotransferase activity, phosphate group as acceptor
Molecular Functionundecaprenyl-diphosphatase activity
Biological ProcessGram-negative-bacterium-type cell outer membrane assembly
Biological Processlipid A biosynthetic process
Biological Processlipopolysaccharide biosynthetic process
Biological Processresponse to bile acid

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipid A 1-diphosphate synthase
  • EC number
  • Alternative names
    • Kdo(2)-lipid A phosphotransferase
    • Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase

Gene names

    • Name
      lpxT
    • Synonyms
      yeiU
    • Ordered locus names
      b2174, JW2162

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P76445
  • Secondary accessions
    • Q2MAR1

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein
Note: Transferase activity takes place on the periplamic side of the inner membrane.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-5Cytoplasmic
Transmembrane6-26Helical
Topological domain27-62Periplasmic
Transmembrane63-83Helical
Topological domain84-90Cytoplasmic
Transmembrane91-111Helical
Topological domain112-145Periplasmic
Topological domain167Cytoplasmic
Transmembrane168-188Helical
Topological domain189-194Periplasmic
Transmembrane195-215Helical
Topological domain216-237Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Deletion of the gene results in the production of LPS containing only the bis-phosphorylated lipid A species.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis190Lack of activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001691601-237Lipid A 1-diphosphate synthase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the LpxT phosphotransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    237
  • Mass (Da)
    26,759
  • Last updated
    1998-07-15 v2
  • Checksum
    A27F9560A1417D09
MIKNLPQIVLLNIVGLALFLSWYIPVNHGFWLPIDADIFYFFNQKLVESKAFLWLVALTNNRAFDGCSLLAMGMLMLSFWLKENAPGRRRIVIIGLVMLLTAVVLNQLGQALIPVKRASPTLTFTDINRVSELLSVPTKDASRDSFPGDHGMMLLIFSAFMWRYFGKVAGLIALIIFVVFAFPRVMIGAHWFTDIIVGSMTVILIGLPWVLLTPLSDRLITFFDKSLPGKNKHFQNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00096
EMBL· GenBank· DDBJ
AAC75235.2
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE76645.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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