ID PCP_BREBN Reviewed; 215 AA. AC C0ZCX0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 75. 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=BBR47_26520; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus. OX NCBI_TaxID=358681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H., RA Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. 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; AP008955; BAH43629.1; -; Genomic_DNA. DR RefSeq; WP_015890949.1; NC_012491.1. DR AlphaFoldDB; C0ZCX0; -. DR SMR; C0ZCX0; -. DR STRING; 358681.BBR47_26520; -. DR MEROPS; C15.001; -. DR KEGG; bbe:BBR47_26520; -. DR eggNOG; COG2039; Bacteria. DR HOGENOM; CLU_043960_4_0_9; -. DR Proteomes; UP000001877; 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 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. 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_1000192222" FT ACT_SITE 80 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417" FT ACT_SITE 143 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417" FT ACT_SITE 167 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417" SQ SEQUENCE 215 AA; 23605 MW; 67322FB9F4ADE688 CRC64; MKTILVTGFD PFGGEIVNPA WESVKELGKI ESDLYKVELR QIPTVFEKSI EHLYAAIEET KPDIVLCIGQ AGGRGDIAVE RVAINVNDAR IPDNEGNQPI DTPIRENGPT GYWSTLPIKA IVHELKQKGI PASISQTAGT YVCNHLFYGL MHYLAEKKAS VRGGFIHIPY LPEQAARQAD QPSMALETIV KGLQLAIETT ISHDRDIVME GGQIS //