Q2FZP6 · MURE_STAA8
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
- GenemurE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids493 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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. Cannot use diaminopimelate as substrate (PubMed:10498701, PubMed:14114846, PubMed:20659527).
Can accept L-ornithine as substrate, but the efficiency is 400-fold lower than that with L-lysine (PubMed:20659527).
Seems to have a role in beta-lactam antibiotic resistance (PubMed:14996801).
Can accept L-ornithine as substrate, but the efficiency is 400-fold lower than that with L-lysine (PubMed:20659527).
Seems to have a role in beta-lactam antibiotic resistance (PubMed:14996801).
Miscellaneous
Expression of this protein in E.coli results in 50% incorporation of L-Lys into the peptidoglycan (which normally contains meso-diaminopimelate instead), leading to abnormal morphological changes and subsequent cell lysis.
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
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.4 mM | UDP-N-acetylmuramoyl-L-Ala-D-Glu | |||||
0.087 mM | UDP-N-acetylmuramoyl-L-Ala-D-Glu | |||||
0.5 mM | L-lysine | |||||
0.55 mM | L-lysine | |||||
37 mM | L-ornithine | |||||
0.3 mM | ATP | |||||
0.53 mM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
5.3 μmol/min/mg | with L-lysine as substrate | ||||
0.87 μmol/min/mg | with L-ornithine as substrate |
pH Dependence
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionQ2FZP6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000012382 | 1-493 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase | |||
Sequence: MDASTLFKKVKVKRVLGSLEQQIDDITTDSRTAREGSIFVASVGYTVDSHKFCQNVADQGCKLVVVNKEQSLPANVTQVVVPDTLRVASILAHTLYDYPSHQLVTFGVTGTNGKTSIATMIHLIQRKLQKNSAYLGTNGFQINETKTKGANTTPETVSLTKKIKEAVDAGAESMTLEVSSHGLVLGRLRGVEFDVAIFSNLTQDHLDFHGTMEAYGHAKSLLFSQLGEDLSKEKYVVLNNDDSFSEYLRTVTPYEVFSYGIDEEAQFMAKNIQESLQGVSFDFVTPFGTYPVKSPYVGKFNISNIMAAMIAVWSKGTSLETIIKAVENLEPVEGRLEVLDPSLPIDLIIDYAHTADGMNKLIDAVQPFVKQKLIFLVGMAGERDLTKTPEMGRVACRADYVIFTPDNPANDDPKMLTAELAKGATHQNYIEFDDRAEGIKHAIDIAEPGDTVVLASKGREPYQIMPGHIKVPHRDDLIGLEAAYKKFGGGPVD | ||||||
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.
Proteomic databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
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
- Length493
- Mass (Da)54,105
- Last updated2006-03-21 v1
- Checksum0D224B23DA5A1390
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000253 EMBL· GenBank· DDBJ | ABD30079.1 EMBL· GenBank· DDBJ | Genomic DNA |