J9W627 · J9W627_LENBU
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
- Genemure3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids511 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Catalytic activity
- UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + ADP + phosphate + H+
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 38 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 114-120 | ATP (UniProtKB | ChEBI) | |||
Binding site | 160-161 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 187 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 195 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase 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 nameUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lentilactobacillus > Lentilactobacillus buchneri subsp. silagei
Accessions
- Primary accessionJ9W627
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 229 | N6-carboxylysine | |||
Post-translational modification
Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 113-332 | Mur ligase central | |||
Domain | 355-483 | Mur ligase C-terminal | |||
Motif | 429-432 | L-lysine recognition motif | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)55,843
- Last updated2012-11-28 v1
- ChecksumF8C19730DA071CDB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003043 EMBL· GenBank· DDBJ | AFS00400.1 EMBL· GenBank· DDBJ | Genomic DNA |