A0A6G8ANN9 · A0A6G8ANN9_9ENTE
- ProteinUDP-N-acetylmuramyl-tripeptide synthetase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids506 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 124-130 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTKGKTT | ||||||
Binding site | 168-169 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 195 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 203 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acid-amino acid ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
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 nameUDP-N-acetylmuramyl-tripeptide synthetase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Vagococcus
Accessions
- Primary accessionA0A6G8ANN9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 237 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 123-328 | Mur ligase central | ||||
Sequence: TGTKGKTTAAYFSKFILDVATQSKTALLSTMETILDGKTATKSLLTTPEAVDLYRMMAEAVSNGMTHLVMEVSSQAYKTQRVYGLDFDVAIFLNISEDHIGTIEHPDFDDYFYCKRQLMTHAKEVIINRNSDFVEIIEEVSQQAGANVTTYGDDSVEADYTFVSSAEGKGKFVVTSTQDSLNLSGDYQINLLGDFNQGNALSAMIA | ||||||
Domain | 350-477 | Mur ligase C-terminal | ||||
Sequence: GRMDTVTTNKGVPIYVDFAHNLLSLQTLLSFVKKEHADRRLVVVIGSTGGKGESRRKDFGNVLSELADVAILTSDDPGTESAKDIAAEIESYLSDRVERLTELNRAFAIKHALETATEKDVIVLAGKG |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)55,622
- Last updated2020-08-12 v1
- ChecksumA953668CA36C1D82
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP049886 EMBL· GenBank· DDBJ | QIL46616.1 EMBL· GenBank· DDBJ | Genomic DNA |