A0A444JF22 · A0A444JF22_9BACT
- ProteinMultifunctional fusion protein
- GenemurF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1042 (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.
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic activity
- UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate + D-alanyl-D-alanine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + ADP + phosphate + H+
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) | |||
Binding site | 123-129 | ATP (UniProtKB | ChEBI) | |||
Binding site | 170-171 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 197 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 205 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | |||
Binding site | 419 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 443-446 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 515 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 519 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | |||
Binding site | 663-669 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | tetrahydrofolylpolyglutamate synthase activity | |
Molecular Function | UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity | |
Molecular Function | UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- EC number
- Alternative names
- Recommended nameUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfobulbaceae > Candidatus Electrothrix
Accessions
- Primary accessionA0A444JF22
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 237 | 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, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 37-109 | Mur ligase N-terminal catalytic | |||
Domain | 122-342 | Mur ligase central | |||
Domain | 375-517 | Mur ligase C-terminal | |||
Motif | 443-446 | Meso-diaminopimelate recognition motif | |||
Domain | 571-648 | Mur ligase N-terminal catalytic | |||
Domain | 661-863 | Mur ligase central | |||
Domain | 886-1017 | Mur ligase C-terminal | |||
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Belongs to the MurCDEF family. MurF subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,042
- Mass (Da)111,645
- Last updated2019-05-08 v1
- MD5 Checksum9C3FB795F1D5BA95D8162EAD50398440
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MTKS01000096 EMBL· GenBank· DDBJ | RWX51700.1 EMBL· GenBank· DDBJ | Genomic DNA |