A0A1E7G5W9 · A0A1E7G5W9_LACLC
- ProteinUDP-N-acetylmuramyl-tripeptide synthetase
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids483 (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 | 43 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 116-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTKGKTT | ||||||
Binding site | 160-161 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 187 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 195 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acid-amino acid ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus > Lactococcus cremoris subsp. cremoris
Accessions
- Primary accessionA0A1E7G5W9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 229 | 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 115-310 | Mur ligase central | ||||
Sequence: TGTKGKTTSAYFAKAILDKMNGGKTALLSTAQTTLDGQNYFKSELTTPESLDLLEMMAKALENGMTHLVMEVSSQAYKTERVYGLTFDVGVFLNISPDHIGPVEHPTLEDYFYCKRQLLKNSRYFVANAEMNHFAIIKEELNERKIPHAFYGADSENKIIESKGLHFVTDGSVSGEFDIRLLGRFNQENALATALA | ||||||
Domain | 332-458 | Mur ligase C-terminal | ||||
Sequence: GRMELLTAKNGAHIYIDYAHNGLSLENLVEVVEDHHAGQLFLVLGSTGNKGESRRKDFGQVIENHPRLNVILTTDDSNRENPKTIADEIASFVSRELDFELDRKFAIKKAISKTQNSDDAVIIAGKG |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length483
- Mass (Da)54,112
- Last updated2017-02-15 v1
- Checksum8BE769D398430CA7