Q81WC7 · MURE_BACAN
- ProteinUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- GenemurE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids491 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Catalytic activity
- ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H+ + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
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 | 108-114 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTT | ||||||
Binding site | 149 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 150-151 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 177 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 185 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 383 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 407-410 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 457 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 461 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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--2,6-diaminopimelate ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionQ81WC7
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000101863 | 1-491 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase | |||
Sequence: MKLHTLVSCLHDFPVVPKENPEITSIEADSRKVKEGSLFVCMKGYTVDSHDFAKQAAAQGAAAIVAERPIDVDVPVVLVKNTFRSLAVLADYFYGQPTHKLHLIGITGTNGKTTTSHIMDEIMRAHGHKTGLIGTINMKIGDETFEVKNTTPDALTLQQTFAKMVEHGVDSTVMEVSSHALDLGRVHGCDYDVAVFTNLTQDHLDYHKTMEEYKHAKGLLFAQLGNSYNHNREKYAVLNNDDAVTVEYMRSTAATVVTYGIDTTSDVMAKDIAMTSGGTTFTLVTPYESVNVTMKLIGKFNVYNVLAATAAGLVSGVSLETIIDVIKELAGVPGRFEVVDGGQNYTVIVDYAHTPDSLENVLKTAKQFAKGDVYCIVGCGGDRDRTKRPIMASVATQYATHAIYTSDNPRSEDPAAILDDMVHGANGNNYEVIIDRKEAIHHAITKAKADDIIIIAGKGHETYQIIGKDVHHFDDREVAKEAITERLNNEE | ||||||
Modified residue | 217 | 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 motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 407-410 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)53,705
- Last updated2003-06-01 v1
- Checksum7E2193B06F881669
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016879 EMBL· GenBank· DDBJ | AAP27779.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE017334 EMBL· GenBank· DDBJ | AAT33170.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE017225 EMBL· GenBank· DDBJ | AAT56067.1 EMBL· GenBank· DDBJ | Genomic DNA |