ID   PCP_STRP6               Reviewed;         215 AA.
AC   Q5XDD4; Q01328;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=M6_Spy0444;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D471 / Serotype M6;
RX   PubMed=1357525; DOI=10.1111/j.1365-2958.1992.tb01378.x;
RA   Cleuziat P., Robert-Baudouy J.;
RT   "Molecular characterization of pcp, the structural gene encoding the
RT   pyrrolidone carboxylyl peptidase from Streptococcus pyogenes.";
RL   Mol. Microbiol. 6:2051-2063(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 3-24; 80-103 AND 190-204, AND MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6;
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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   -!- MASS SPECTROMETRY: Mass=23131.60; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.3};
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; X65717; CAA46633.1; -; Genomic_DNA.
DR   EMBL; CP000003; AAT86579.1; -; Genomic_DNA.
DR   PIR; S24717; S24717.
DR   RefSeq; WP_002994169.1; NC_006086.1.
DR   AlphaFoldDB; Q5XDD4; -.
DR   SMR; Q5XDD4; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; AAT86579; AAT86579; M6_Spy0444.
DR   GeneID; 57852244; -.
DR   KEGG; spa:M6_Spy0444; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; KLAYNHK; -.
DR   Proteomes; UP000001167; 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; -; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184744"
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