A0A6A1Z7X8 · A0A6A1Z7X8_9LACO
- ProteinPhospho-N-acetylmuramoyl-pentapeptide-transferase
- GenemraY
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids322 (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
- UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + di-trans,octa-cis-undecaprenyl phosphate = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus
Accessions
- Primary accessionA0A6A1Z7X8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 6-26 | Helical | ||||
Sequence: ASCIALVSSLVLTVIFIPLLI | ||||||
Transmembrane | 54-75 | Helical | ||||
Sequence: TMGGTVFVIAAVISVIWVAAMQ | ||||||
Transmembrane | 81-102 | Helical | ||||
Sequence: VIWILVISLLGYGIIGFLDDGI | ||||||
Transmembrane | 114-133 | Helical | ||||
Sequence: AWQKLALQIIIAILIVLIAT | ||||||
Transmembrane | 139-164 | Helical | ||||
Sequence: FGLYIPFAGVVHSLVLFVAFIIFWLV | ||||||
Transmembrane | 176-195 | Helical | ||||
Sequence: LDGLATGLSVVAYGTYAYIA | ||||||
Transmembrane | 201-220 | Helical | ||||
Sequence: FAVLAFCMSVIGGLIAFFIF | ||||||
Transmembrane | 227-248 | Helical | ||||
Sequence: IFMGDAGSLALGGGLATISIML | ||||||
Transmembrane | 254-275 | Helical | ||||
Sequence: LLLVGIVFVCETASVILQVISF | ||||||
Transmembrane | 304-321 | Helical | ||||
Sequence: IVFWLVGLIGSILYLVIW |
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
- Length322
- Mass (Da)35,537
- Last updated2020-06-17 v1
- Checksum314CE03F01F59958