ID PCP_STRPZ Reviewed; 215 AA. AC B5XK96; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 78. 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}; GN OrderedLocusNames=Spy49_0425c; OS Streptococcus pyogenes serotype M49 (strain NZ131). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=471876; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NZ131; RX PubMed=18820018; DOI=10.1128/jb.00672-08; RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B., RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.; RT "Genome sequence of a nephritogenic and highly transformable M49 strain of RT Streptococcus pyogenes."; RL J. Bacteriol. 190:7773-7785(2008). 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}. 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; CP000829; ACI60758.1; -; Genomic_DNA. DR RefSeq; WP_002994169.1; NC_011375.1. DR AlphaFoldDB; B5XK96; -. DR SMR; B5XK96; -. DR MEROPS; C15.001; -. DR KEGG; soz:Spy49_0425c; -. DR HOGENOM; CLU_043960_4_0_9; -. DR Proteomes; UP000001039; 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; Thiol protease. FT CHAIN 1..215 FT /note="Pyrrolidone-carboxylate peptidase" FT /id="PRO_1000124003" 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 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 //