A0A1S2ML75 · A0A1S2ML75_9STAP
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids494 (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
- ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H+ + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 30 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 110-116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTS | ||||||
Binding site | 151 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 152-153 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 179 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 187 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A1S2ML75
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 219 | 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, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-79 | Mur ligase N-terminal catalytic | ||||
Sequence: INDITTDSRTAKQGSVFIASKGYTVDSHKFCQDVVDKGCQVVVVSEEQTLNGDVTQV | ||||||
Domain | 108-311 | Mur ligase central | ||||
Sequence: VTGTNGKTSIATMIHHIYRKLDKSSAYLGTNGFQINENKSKGANTTPETVSLTKKINEAVENKAEAMTLEVSSHGLSLGRLRGVDFDVAIFSNLTQDHLDFHGTMEAYGHAKSLLFSQLGEDLSKEKYAVLNNDDTFSEYLGAVTPFETFTYGINHKAQFMAEQINESLQGVHFKFVTPLGRFEVKSPYVGMFNVSNIMAAMIA | ||||||
Domain | 334-458 | Mur ligase C-terminal | ||||
Sequence: GRLEVLDPSLPIDLIIDYAHTADGMDKLIDAVKPFAKQKLIFLCGMAGERDMGKTPEMGRVACRADYVIFTPDNPANDDPKKLTAELAKGATHHNYIEFEDRAEGIRHAIDVAEPGDTVVLASKG | ||||||
Motif | 406-409 | L-lysine recognition motif | ||||
Sequence: DNPA |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)54,412
- Last updated2017-04-12 v1
- ChecksumE2CBC8AE4D7FC0FE