ID   PCP_PSEFL               Reviewed;         213 AA.
AC   P42673;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase;
DE            EC=3.4.19.3;
DE   AltName: Full=5-oxoprolyl-peptidase;
DE   AltName: Full=Pyroglutamyl-peptidase I;
DE            Short=PGP-I;
DE            Short=Pyrase;
GN   Name=pcp;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MFO;
RX   PubMed=7909543; DOI=10.1128/jb.176.9.2569-2576.1994;
RA   Gonzales T., Robert-Baudouy J.;
RT   "Characterization of the pcp gene of Pseudomonas fluorescens and of its
RT   product, pyrrolidone carboxyl peptidase (Pcp).";
RL   J. Bacteriol. 176:2569-2576(1994).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal pyroglutamyl group from a
CC         polypeptide, the second amino acid generally not being Pro.;
CC         EC=3.4.19.3;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; X75919; CAA53519.1; -; Genomic_DNA.
DR   PIR; A55583; A55583.
DR   AlphaFoldDB; P42673; -.
DR   SMR; P42673; -.
DR   MEROPS; C15.001; -.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00501; Peptidase_C15; 1.
DR   Gene3D; 3.40.630.20; -; 1.
DR   HAMAP; MF_00417; Pyrrolid_peptidase; 1.
DR   InterPro; IPR000816; Peptidase_C15.
DR   InterPro; IPR016125; Peptidase_C15-like.
DR   InterPro; IPR036440; Peptidase_C15-like_sf.
DR   InterPro; IPR029762; PGP-I_bact-type.
DR   InterPro; IPR033694; PGPEP1_Cys_AS.
DR   InterPro; IPR033693; PGPEP1_Glu_AS.
DR   PANTHER; PTHR23402; PTHR23402; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; SSF53182; 1.
DR   TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR   PROSITE; PS01334; PYRASE_CYS; 1.
DR   PROSITE; PS01333; PYRASE_GLU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..213
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184728"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  22438 MW;  D63979DC51AC3AA3 CRC64;
     MRIVLLTGFE PFDQDPVNPS WEAVRQLDGV QLGSDVKIVA RRLPCAFATA GECLTRLIDE
     LHPAMVIATG LGPGRSDISV ERVAININDA RIPDNLGEQP IDTAVVADGP AAFFTTLPIK
     AMVKAVREAG IAASVSQTAG TFVCNQVFYL LQHALAGSGV RSGFIHVPFL PEQVAGSQRP
     SMALDAMVAG LQAAVLTAWH TPVDVKEAGG QVS