ID   PCP_STAAU               Reviewed;         212 AA.
AC   Q53596;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 103.
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   Staphylococcus aureus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FDA 574;
RX   PubMed=8529900; DOI=10.1016/0378-1119(95)00561-0;
RA   Patti J.M., Schneider A., Garza N., Boles J.O.;
RT   "Isolation and characterization of pcp, a gene encoding a pyrrolidone
RT   carboxyl peptidase in Staphylococcus aureus.";
RL   Gene 166:95-99(1995).
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: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; U19770; AAA99709.1; -; Genomic_DNA.
DR   PIR; JC4511; JC4511.
DR   AlphaFoldDB; Q53596; -.
DR   SMR; Q53596; -.
DR   MEROPS; C15.001; -.
DR   BioCyc; MetaCyc:MONOMER-20361; -.
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; Peptidase C15, pyroglutamyl peptidase I-like; 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   NCBIfam; TIGR00504; pyro_pdase; 1.
DR   PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; RE07960P; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 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..212
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184736"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23227 MW;  D646E167B951B832 CRC64;
     MHILVTGFAP FDNQDINPSW EAVTQLENII GTHTIDKLKL PTSFKKVDTI INKTLASNHY
     DVVLAIGQAG GRNAITPERV AINIDDARIP DNDDFQPIDQ AIHLDGAPRY FSNLPVKAMT
     QSVINQGLPG ALSNSAGTFV CNHVLYHLGY LQDKHYPHLR FGFIHVPYIP EQVVGKSDTP
     SMPLEQIVAG LTAAIEAISD HDDLRIALGT TE
//