A0A6C7I6B4 · A0A6C7I6B4_SALTD
- ProteinPhospho-N-acetylmuramoyl-pentapeptide-transferase
- GenemraY
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids360 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic activity
- di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | phospho-N-acetylmuramoyl-pentapeptide-transferase activity | |
Molecular Function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospho-N-acetylmuramoyl-pentapeptide-transferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A6C7I6B4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 20-40 | Helical | ||||
Sequence: SYLTFRAIVSLLTALFISLWM | ||||||
Transmembrane | 73-90 | Helical | ||||
Sequence: TMGGIMILTSIVISVLLW | ||||||
Transmembrane | 96-114 | Helical | ||||
Sequence: PYVWCVLVVLIGYGIIGFV | ||||||
Transmembrane | 134-152 | Helical | ||||
Sequence: YFWMSVIALGVAFALYLVG | ||||||
Transmembrane | 172-193 | Helical | ||||
Sequence: LGLFYILLSYFVIVGTGNAVNL | ||||||
Transmembrane | 200-219 | Helical | ||||
Sequence: LAIMPTVFVAAGFALVAWAT | ||||||
Transmembrane | 239-256 | Helical | ||||
Sequence: LVIVCTAIVGAGLGFLWF | ||||||
Transmembrane | 263-284 | Helical | ||||
Sequence: VFMGDVGSLALGGALGIIAVLL | ||||||
Transmembrane | 290-311 | Helical | ||||
Sequence: LVIMGGVFVVETLSVILQVGSF | ||||||
Transmembrane | 338-357 | Helical | ||||
Sequence: VIVRFWIISLMLVLIGLATL |
Keywords
- Cellular component
Structure
Family & Domains
Sequence similarities
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length360
- Mass (Da)40,023
- Last updated2020-06-17 v1
- Checksum3DD634C207ACFD94
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FN424405 EMBL· GenBank· DDBJ | CBG23147.1 EMBL· GenBank· DDBJ | Genomic DNA |