P24171 · DCP_ECOLI

Function

function

Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides.

Catalytic activity

  • Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly.
    EC:3.4.15.5 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

168150100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site470Zn2+ (UniProtKB | ChEBI); catalytic
Active site471
Binding site474Zn2+ (UniProtKB | ChEBI); catalytic
Binding site477Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentouter membrane-bounded periplasmic space
Molecular Functioncarboxypeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dipeptidyl carboxypeptidase
  • EC number
  • Alternative names
    • Peptidyl-dipeptidase Dcp

Gene names

    • Name
      dcp
    • Ordered locus names
      b1538, JW1531

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P24171
  • Secondary accessions
    • P78305

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Unable to grow on N-benzoyl-Gly-His-Leu as a nitrogen source.

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000781572-681Dipeptidyl carboxypeptidase

Proteomic databases

Interaction

Protein-protein interaction databases

Chemistry

Family & Domains

Sequence similarities

Belongs to the peptidase M3 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    681
  • Mass (Da)
    77,516
  • Last updated
    2007-01-23 v4
  • Checksum
    659C5FD659566391
MTTMNPFLVQSTLPYLAPHFDQIANHHYRPAFDEGMQQKRAEIAAIALNPQMPDFNNTILALEQSGELLTRVTSVFFAMTAAHTNDELQRLDEQFSAELAELANDIYLNGELFARVDAVWQRRESLGLDSESIRLVEVIHQRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIAQLAGMSEQEIALAAEAAREKGLDNKWLIPLLNTTQQPALAEMRDRATREKLFIAGWTRAEKNDANDTRAIIQRLVEIRAQQATLLGFPHYAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDKQQGGFSAQPWDWAFYAEQVRREKFDLDEAQLKPYFELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLALFYGDFFARDSKSGGAWMGNFVEQSTLNKTHPVIYNVCNYQKPAAGEPALLLWDDVITLFHEFGHTLHGLFARQRYATLSGTNTPRDFVEFPSQINEHWATHPQVFARYARHYQSGAAMPDELQQKMRNASLFNKGYEMSELLSAALLDMRWHCLEENEAMQDVDDFELRALVAENMDLPAIPPRYRSSYFAHIFGGGYAAGYYAYLWTQMLADDGYQWFVEQGGLTRENGLRFREAILSRGNSEDLERLYRQWRGKAPKIMPMLQHRGLNI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict139-140in Ref. 1; CAA41014

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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