P76445 · LPXT_ECOLI
- ProteinLipid A 1-diphosphate synthase
- GenelpxT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) + di-trans,octa-cis-undecaprenyl diphosphate = (Kdo)2-lipid A 1-diphosphate + di-trans,octa-cis-undecaprenyl phosphate
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
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | phosphotransferase activity, phosphate group as acceptor | |
Molecular Function | undecaprenyl-diphosphatase activity | |
Biological Process | Gram-negative-bacterium-type cell outer membrane assembly | |
Biological Process | lipid A biosynthetic process | |
Biological Process | lipopolysaccharide biosynthetic process | |
Biological Process | response to bile acid |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipid A 1-diphosphate synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP76445
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-5 | Cytoplasmic | ||||
Sequence: MIKNL | ||||||
Transmembrane | 6-26 | Helical | ||||
Sequence: PQIVLLNIVGLALFLSWYIPV | ||||||
Topological domain | 27-62 | Periplasmic | ||||
Sequence: NHGFWLPIDADIFYFFNQKLVESKAFLWLVALTNNR | ||||||
Transmembrane | 63-83 | Helical | ||||
Sequence: AFDGCSLLAMGMLMLSFWLKE | ||||||
Topological domain | 84-90 | Cytoplasmic | ||||
Sequence: NAPGRRR | ||||||
Transmembrane | 91-111 | Helical | ||||
Sequence: IVIIGLVMLLTAVVLNQLGQA | ||||||
Topological domain | 112-145 | Periplasmic | ||||
Sequence: LIPVKRASPTLTFTDINRVSELLSVPTKDASRDS | ||||||
Topological domain | 167 | Cytoplasmic | ||||
Sequence: K | ||||||
Transmembrane | 168-188 | Helical | ||||
Sequence: VAGLIALIIFVVFAFPRVMIG | ||||||
Topological domain | 189-194 | Periplasmic | ||||
Sequence: AHWFTD | ||||||
Transmembrane | 195-215 | Helical | ||||
Sequence: IIVGSMTVILIGLPWVLLTPL | ||||||
Topological domain | 216-237 | Cytoplasmic | ||||
Sequence: SDRLITFFDKSLPGKNKHFQNK |
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 190 | Lack of activity. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000169160 | 1-237 | Lipid A 1-diphosphate synthase | |||
Sequence: MIKNLPQIVLLNIVGLALFLSWYIPVNHGFWLPIDADIFYFFNQKLVESKAFLWLVALTNNRAFDGCSLLAMGMLMLSFWLKENAPGRRRIVIIGLVMLLTAVVLNQLGQALIPVKRASPTLTFTDINRVSELLSVPTKDASRDSFPGDHGMMLLIFSAFMWRYFGKVAGLIALIIFVVFAFPRVMIGAHWFTDIIVGSMTVILIGLPWVLLTPLSDRLITFFDKSLPGKNKHFQNK |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length237
- Mass (Da)26,759
- Last updated1998-07-15 v2
- ChecksumA27F9560A1417D09
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC75235.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76645.1 EMBL· GenBank· DDBJ | Genomic DNA |