P24171 · DCP_ECOLI
- ProteinDipeptidyl carboxypeptidase
- Genedcp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids681 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion.
Activity regulation
Stimulated by Mn2+, Mg2+, Co2+ and Ca2+, inhibited by Cu2+, Ni2+, Zn2+, chymostatin and 1,10-phenanthroline.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDipeptidyl carboxypeptidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP24171
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000078157 | 2-681 | Dipeptidyl carboxypeptidase | |||
Sequence: TTMNPFLVQSTLPYLAPHFDQIANHHYRPAFDEGMQQKRAEIAAIALNPQMPDFNNTILALEQSGELLTRVTSVFFAMTAAHTNDELQRLDEQFSAELAELANDIYLNGELFARVDAVWQRRESLGLDSESIRLVEVIHQRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIAQLAGMSEQEIALAAEAAREKGLDNKWLIPLLNTTQQPALAEMRDRATREKLFIAGWTRAEKNDANDTRAIIQRLVEIRAQQATLLGFPHYAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDKQQGGFSAQPWDWAFYAEQVRREKFDLDEAQLKPYFELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLALFYGDFFARDSKSGGAWMGNFVEQSTLNKTHPVIYNVCNYQKPAAGEPALLLWDDVITLFHEFGHTLHGLFARQRYATLSGTNTPRDFVEFPSQINEHWATHPQVFARYARHYQSGAAMPDELQQKMRNASLFNKGYEMSELLSAALLDMRWHCLEENEAMQDVDDFELRALVAENMDLPAIPPRYRSSYFAHIFGGGYAAGYYAYLWTQMLADDGYQWFVEQGGLTRENGLRFREAILSRGNSEDLERLYRQWRGKAPKIMPMLQHRGLNI |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length681
- Mass (Da)77,516
- Last updated2007-01-23 v4
- Checksum659C5FD659566391
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 139-140 | in Ref. 1; CAA41014 | ||||
Sequence: IH → LL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X57947 EMBL· GenBank· DDBJ | CAA41014.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74611.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA15228.1 EMBL· GenBank· DDBJ | Genomic DNA |