ID   PCP_STAAS               Reviewed;         212 AA.
AC   Q6G5Y4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN   Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=SAS2576;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00417};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00417}.
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DR   EMBL; BX571857; CAG44393.1; -; Genomic_DNA.
DR   RefSeq; WP_000547833.1; NC_002953.3.
DR   AlphaFoldDB; Q6G5Y4; -.
DR   SMR; Q6G5Y4; -.
DR   MEROPS; C15.001; -.
DR   KEGG; sas:SAS2576; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; KLAYNHK; -.
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..212
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184735"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   212 AA;  23167 MW;  BBC76CD8FC43ACBC CRC64;
     MHILVTGFAP FDNQNINPSW EAVTQLEDII GTHTIDKLKL PTSFKKVDNI INKTLASNHY
     DVVLAIGQAG GRNAITPERV AINIDDARIP DNDDFQPIDQ AIHLDGAPAY FSNLPVKAMT
     QSIINQGLPG ALSNSAGTFV CNHTLYHLGY LQDKHYPHLR FGFIHVPYIP EQVIGKPDTP
     SMPLEKIVAG LTAAIEAISN DEDLHLALGT TE