Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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PepX_N X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal

SMART accession number:	SM00940
Description:	This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, with the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction (PUBMED:12377124).
Interpro abstract (IPR015251):	This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, with the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N terminus also forms a small parallel beta sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction [ (PUBMED:12377124) ].
GO process:	proteolysis (GO:0006508)
GO function:	dipeptidyl-peptidase activity (GO:0008239)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 558 PepX_N domains in 558 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing PepX_N domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with PepX_N domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing PepX_N domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Rigolet P, Mechin I, Delage MM, Chich JF
  • The structural basis for catalysis and specificity of the X-prolyldipeptidyl aminopeptidase from Lactococcus lactis.
  • Structure. 2002; 10: 1383-94
  • Display abstract

  • The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis isa dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the Nterminus of peptides. The structure of the enzyme was solved at 2.2 Aresolution and provides a model for the peptidase family S15. Each monomeris composed of four domains. The larger one presents an alpha/betahydrolase fold and comprises the active site serine. The specificitypocket is mainly built by residues from a small helical domain which is,together with the N-terminal domain, essential for dimerization. AC-terminal moiety probably plays a role in the tropism of X-PDAP towardthe cellular membrane. These results give new insights for furtherexploration of the role of the enzymes of the SC clan.

• Structure (3D structures containing this domain)

• 3D Structures of PepX_N domains in PDB

  PDB code	Main view	Title
  1lns		Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

• Links (links to other resources describing this domain)

• PFAM	PepX_N
  INTERPRO	IPR015251

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