A0A4V3A3S0 · A0A4V3A3S0_9LACO
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids515 (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) | ||||
Sequence: S | ||||||
Binding site | 115-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTKGKTT | ||||||
Binding site | 161-162 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 188 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 196 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
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 > Secundilactobacillus
Accessions
- Primary accessionA0A4V3A3S0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 230 | N6-carboxylysine | ||||
Sequence: K |
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 | 114-334 | Mur ligase central | ||||
Sequence: TGTKGKTTSAYFSRGILQKSTQEKTALFSTIDRFVGSKPDQHFKSHLTTPESLDLFHDMRTAVNNGMTHLVMEVSSQAYKKNRVYNLKYDVGVFLNISPDHIGANEHPTFADYLHCKEQLLVNSKICVINAETDHLEDVYEAAKATSQPDDIYLFARKGGKKQVALPLDFEFENQSETLHGSNFTLRSISQKAKELSLDNQYELSLPGDYNESNAASAIIA | ||||||
Domain | 356-484 | Mur ligase C-terminal | ||||
Sequence: GRMEFVKTKNHGTVYIDYAHNYGSMKSLLAFLRKQTNAGRVIALTGSTGNKGESRRKGFGQALSEEADVAFLTADDPAFESPQAIAEEIDSYIDHDKVEVHFNMDRISAIKEAIQTSTNQDIVVLAGKG | ||||||
Motif | 430-433 | L-lysine recognition motif | ||||
Sequence: DDPA |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length515
- Mass (Da)56,866
- Last updated2019-07-31 v1
- ChecksumA5060417E29C26C5
Keywords
- Technical term