A0A353NKH3 · A0A353NKH3_9BACT
- ProteinMultifunctional fusion protein
- GenemurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1014 (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
- ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H+ + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
Cofactor
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 40 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 125-131 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTNGKTT | ||||||
Binding site | 172-173 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 199 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 205 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 207 | UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 414 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 438-441 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: DNPR | ||||||
Binding site | 506 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 510 | meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 649-655 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSCGKTT |
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
Accessions
- Primary accessionA0A353NKH3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 239 | 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, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-111 | Mur ligase N-terminal catalytic | ||||
Sequence: VTSVTSDSRTVTPESLFVALSGTGTDGHKYLENAIGNGCTAVLCEAGRVSEDLLQKLQAVVIETPDTNKAYAAVAANFY | ||||||
Domain | 123-337 | Mur ligase central | ||||
Sequence: VTGTNGKTTVTYLLEQVLLQAGHGVGVIGTVNNRYTLADGTKKIIGTRFTTPEAMLLQQLLREMIDCGVEYVVMEVSSHALAQRRVGELSFAVVAFTNLTRDHLDYHLDMDDYFRAKTKLFTEYLVEGGRAVLPVAEARPESPAWLATLHEICAQAGKKVVSWGEGENASVSLVNHTAGLTRTDLVLQTPSGQHRFSTPLVGRFNIDNILTVVAM | ||||||
Domain | 375-508 | Mur ligase C-terminal | ||||
Sequence: APAVFVDYAHTPDALEKVLTTAAALPHRQLIGVFGCGGDRDKGKRPVMGEIATRLCDIAIVTDDNPRTEDPEAIVEQILAGIQNRTEYVKDSSWLAGRKPMDRGCTVIRDRKTAIASAIKSGGPDDIVVIAGKG | ||||||
Motif | 438-441 | Meso-diaminopimelate recognition motif | ||||
Sequence: DNPR | ||||||
Domain | 647-848 | Mur ligase central | ||||
Sequence: ITGSCGKTTVKEMIAAILARKWPEGPDNPIGCVLKTRGNFNNIIGLPISLLPLDLSHRAAVMEMGMNMPGELTRLAEIADPDISIITNIHGAHLLGLGTIEGVARAKEELFAGTKQSGTLVINLDDLWVRQFAGKYPQRKVTFAVRKEDHASPPDFWASDVVQDNGGAIIFTMHYRQETAEIHLFTAGLHNVANALAAAATA | ||||||
Domain | 871-1001 | Mur ligase C-terminal | ||||
Sequence: RMEILYPKAGFILINDTYNANPASMAAGLRTLKQMARKSTTAIIGDMRELGEASAQAHFDIGRLIAELAIDRVGVVGDFRDDVQRGAIAHGCPAESIRTFADKDAAVSWIKEMIATKRIGKDDLILIKASR |
Sequence similarities
Belongs to the MurCDEF family. MurE subfamily.
Belongs to the MurCDEF family. MurF subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,014
- Mass (Da)108,774
- Last updated2018-11-07 v1
- ChecksumF24B7B12425907AE