F1VYP7 · F1VYP7_9BURK
- Proteinserine-type D-Ala-D-Ala carboxypeptidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids403 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Catalytic activity
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 79 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 82 | Proton acceptor | ||||
Sequence: K | ||||||
Active site | 141 | |||||
Sequence: S | ||||||
Binding site | 243 | substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameserine-type D-Ala-D-Ala carboxypeptidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae
Accessions
- Primary accessionF1VYP7
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 297-387 | Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-terminal | ||||
Sequence: FDTVKLYGKGQPVETPPVWKGSEKTIKIGFTQDIYVTVAKGVAAKMKPVLERKDPLVAPIAANSKVGMMKMMVDGKSIAEFPILALENVNE |
Sequence similarities
Belongs to the peptidase S11 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)43,928
- Last updated2011-05-31 v1
- Checksum33B7AEB29D97D10A
Keywords
- Technical term