A0A7Z1EJI7 · A0A7Z1EJI7_SHIFL
- ProteinLipid A 1-diphosphate synthase
- GenelpxT
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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).
Catalytic activity
- an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + di-trans,octa-cis-undecaprenyl diphosphate = an alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A 1-diphosphate + di-trans,octa-cis-undecaprenyl phosphate
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 |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Shigella
Accessions
- Primary accessionA0A7Z1EJI7
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 transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 7-24 | Helical | ||||
Sequence: QIVLLNIVGLALFLSWYI | ||||||
Transmembrane | 63-81 | Helical | ||||
Sequence: AFDGCSLLAMGMLMLSFWL | ||||||
Transmembrane | 93-113 | Helical | ||||
Sequence: IIGLVMLLTAVVLNQLGQALI | ||||||
Transmembrane | 161-182 | Helical | ||||
Sequence: MWRYFGKVAGLIALIIFVVFAF | ||||||
Transmembrane | 191-212 | Helical | ||||
Sequence: WFTDIIVGSMTVILIGLPWVLL |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 94-210 | Phosphatidic acid phosphatase type 2/haloperoxidase | ||||
Sequence: IGLVMLLTAVVLNQLGQALIPVKRASPTLTFTDINRVSELLSVPTKDASRDSFPGDHGMMLLIFSAFMWRYFGKVAGLIALIIFVVFAFPRVMIGAHWFTDIIVGSMTVILIGLPWV |
Sequence similarities
Belongs to the LpxT phosphotransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length237
- Mass (Da)26,759
- Last updated2021-06-02 v1
- ChecksumA27F9560A1417D09
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NIYV01000063 EMBL· GenBank· DDBJ | PAY87254.1 EMBL· GenBank· DDBJ | Genomic DNA |