ID   PCP_STRP1               Reviewed;         215 AA.
AC   P68896; Q01328; Q490D3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 127.
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; OrderedLocusNames=SPy_0506, M5005_Spy0417;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004092; AAK33506.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51035.1; -; Genomic_DNA.
DR   RefSeq; NP_268785.1; NC_002737.2.
DR   AlphaFoldDB; P68896; -.
DR   SMR; P68896; -.
DR   MEROPS; C15.001; -.
DR   PaxDb; 1314-HKU360_00440; -.
DR   KEGG; spy:SPy_0506; -.
DR   KEGG; spz:M5005_Spy0417; -.
DR   PATRIC; fig|160490.10.peg.432; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; VCNHVFY; -.
DR   Proteomes; UP000000750; Chromosome.
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; Reference proteome; Thiol protease.
FT   CHAIN           1..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184742"
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   215 AA;  23132 MW;  2D9E727A09704A69 CRC64;
     MKILVTGFDP FGGEAINPAL EAIKKLPATI HGAEIKCIEV PTVFQKSADV LQQHIESFQP
     DAVLCIGQAG GRTGLTPERV AINQDDARIP DNEGNQPIDT PIRADGKAAY FSTLPIKAMV
     AAIHQAGLPA SVSNTAGTFV CNHLMYQALY LVDKYCPNAK AGFMHIPFMM EQVVDKPNTA
     AMNLDDITRG IEAAIFAIVD FKDRSDLKRV GGATH
//