A0A2B2LIJ4 · A0A2B2LIJ4_BACCE
- ProteinUDP-N-acetylmuramyl-tripeptide synthetase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids493 (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 | 30 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 111-117 | ATP (UniProtKB | ChEBI) | |||
Binding site | 180 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 188 | 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 | tetrahydrofolylpolyglutamate synthase 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-acetylmuramyl-tripeptide synthetase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionA0A2B2LIJ4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 220 | N6-carboxylysine | |||
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 | 22-82 | Mur ligase N-terminal catalytic | |||
Domain | 109-315 | Mur ligase central | |||
Domain | 337-465 | Mur ligase C-terminal | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length493
- Mass (Da)54,820
- Last updated2017-12-20 v1
- Checksum45E6BCFB9FBB3133
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NVAP01000051 EMBL· GenBank· DDBJ | PFQ42595.1 EMBL· GenBank· DDBJ | Genomic DNA |