B4RFS3 · MRAY_PHEZH
- ProteinPhospho-N-acetylmuramoyl-pentapeptide-transferase
- GenemraY
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids369 (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.
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 > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Phenylobacterium
Accessions
- Primary accessionB4RFS3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 30-50 | Helical | ||||
Sequence: LAIFTAQFVVVAMGSRFIRWM | ||||||
Transmembrane | 74-94 | Helical | ||||
Sequence: GTPTMGGVMILAGLLVGTLLW | ||||||
Transmembrane | 97-117 | Helical | ||||
Sequence: LSNPYVWAVVLVTAGYGLLGF | ||||||
Transmembrane | 136-156 | Helical | ||||
Sequence: IRLALEAFIAMAAVLIIIVFA | ||||||
Transmembrane | 177-197 | Helical | ||||
Sequence: YFVDLSWGYLLFGAFIIVGAA | ||||||
Transmembrane | 208-228 | Helical | ||||
Sequence: GLATVPVMIAAAAYGLIAYLV | ||||||
Transmembrane | 244-264 | Helical | ||||
Sequence: GVGEIAVFCGALIGSGLGFLW | ||||||
Transmembrane | 272-292 | Helical | ||||
Sequence: IFMGDTGSLALGGAVGAVAVA | ||||||
Transmembrane | 297-317 | Helical | ||||
Sequence: IVLAIIGGLFVAETLSVIIQV | ||||||
Transmembrane | 346-366 | Helical | ||||
Sequence: TVVIRFWIVAIMLALVGLATL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000090654 | 1-369 | Phospho-N-acetylmuramoyl-pentapeptide-transferase | |||
Sequence: MFYWLYEQFAASGYVPILNLLKYQTFRTGLAIFTAQFVVVAMGSRFIRWMQAKQGKGQPIRAEGIERHVIEKAGTPTMGGVMILAGLLVGTLLWSDLSNPYVWAVVLVTAGYGLLGFTDDYAKVTRQTTAGVSGKIRLALEAFIAMAAVLIIIVFAQKPPENPELLTSVTFPIFKQYFVDLSWGYLLFGAFIIVGAANAVNFTDGLDGLATVPVMIAAAAYGLIAYLVGNYVFSNYLQLHFVPGVGEIAVFCGALIGSGLGFLWYNAPPAKIFMGDTGSLALGGAVGAVAVATRHEIVLAIIGGLFVAETLSVIIQVAWFKRTGRRIFLMAPIHHHFEKLGWSESTVVIRFWIVAIMLALVGLATLKLR |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)40,011
- Last updated2008-09-23 v1
- ChecksumD72E790E38B7BC10
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000747 EMBL· GenBank· DDBJ | ACG78736.1 EMBL· GenBank· DDBJ | Genomic DNA |