Sequence of PPEP1_CLOD6
EC Number:3.4.24.89
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues
Other sequences found for EC No. 3.4.24.89
General information:
Sequence
0 MRPSKKLLIA IISIFLISSV PVSAHADSTT IQQNKDTLSQ IVVFPTGNYD KNEANAMVNR
60 LANIDGKYLN ALKQNNLKIK LLSGKLTDEK EYAYLKGVVP KGWEGTGKTW DDVPGLGGST
120 VALRIGFSNK GKGHDAINLE LHETAHAIDH IVLNDISKSA QFKQIFAKEG RSLGNVNYLG
180 VYPEEFFAES FAYYYLNQDT NSKLKSACPQ TYSFLQNLAK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
843192
Sebaihia M.,Wren B.W.,Mullany P.,Fairweather N.F.,Minton N.,Stabler R.,Thomson N.R.,Roberts A.P.,Cerdeno-Tarraga A.M.,Wang H.,Holden M.T.G.,Wright A.,Churcher C.,Quail M.A.,Baker S.,Bason N.,Brooks K.,Chillingworth T.,Cronin A.,Davis P.,Dowd L.,Fraser A.,Feltwell T.,Hance Z.,Holroyd S.,Jagels K.,Moule S.,Mungall K.,Price C.,Rabbinowitsch E.,Sharp S.,Simmonds M.,Stevens K.,Unwin L.,Whithead S.,Dupuy B.,Dougan G.,Barrell B.,Parkhill J.
The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome.
Nat. Genet.
38
779-786
2006
843193
Soutourina O.A.,Monot M.,Boudry P.,Saujet L.,Pichon C.,Sismeiro O.,Semenova E.,Severinov K.,Le Bouguenec C.,Coppee J.Y.,Dupuy B.,Martin-Verstraete I.
Genome-wide identification of regulatory RNAs in the human pathogen Clostridium difficile.
PLoS Genet.
9
0-0
2013
843194
Cafardi V.,Biagini M.,Martinelli M.,Leuzzi R.,Rubino J.T.,Cantini F.,Norais N.,Scarselli M.,Serruto D.,Unnikrishnan M.
Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins.
PLoS ONE
8
0-0
2013
843195
Hensbergen P.J.,Klychnikov O.I.,Bakker D.,van Winden V.J.,Ras N.,Kemp A.C.,Cordfunke R.A.,Dragan I.,Deelder A.M.,Kuijper E.J.,Corver J.,Drijfhout J.W.,van Leeuwen H.C.
A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins.
Mol. Cell. Proteomics
13
1231-1244
2014
843196
Hensbergen P.J.,Klychnikov O.I.,Bakker D.,Dragan I.,Kelly M.L.,Minton N.P.,Corver J.,Kuijper E.J.,Drijfhout J.W.,van Leeuwen H.C.
Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831.
FEBS Lett.
589
3952-3958
2015
843197
Peltier J.,Shaw H.A.,Couchman E.C.,Dawson L.F.,Yu L.,Choudhary J.S.,Kaever V.,Wren B.W.,Fairweather N.F.
Cyclic diGMP regulates production of sortase substrates of Clostridium difficile and their surface exposure through ZmpI protease-mediated cleavage.
J. Biol. Chem.
290
24453-24469
2015
843198
Corver J.,Cordo' V.,van Leeuwen H.C.,Klychnikov O.I.,Hensbergen P.J.
Covalent attachment and Pro-Pro endopeptidase (PPEP-1)-mediated release of Clostridium difficile cell surface proteins involved in adhesion.
Mol. Microbiol.
105
663-673
2017
843199
Klychnikov O.I.,Shamorkina T.M.,Weeks S.D.,van Leeuwen H.C.,Corver J.,Drijfhout J.W.,van Veelen P.A.,Sluchanko N.N.,Strelkov S.V.,Hensbergen P.J.
Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.
J. Biol. Chem.
293
11154-11165
2018
843200
Schacherl M.,Pichlo C.,Neundorf I.,Baumann U.
Structural basis of proline-proline peptide bond specificity of the metalloprotease Zmp1 implicated in motility of Clostridium difficile.
Structure
23
1632-1642
2015
