ID   PCP_LACLM               Reviewed;         215 AA.
AC   O87765; A2RJ15; Q9L9P5; Q9R805;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=llmg_0663;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9733685; DOI=10.1128/jb.180.18.4834-4842.1998;
RA   Daveran-Mingot M.L., Campo N., Ritzenthaler P., le Bourgeois P.;
RT   "A natural large chromosomal inversion in Lactococcus lactis is mediated by
RT   homologous recombination between two insertion sequences.";
RL   J. Bacteriol. 180:4834-4842(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Buist G., Haandrikman A.J., Benus G., Feenstra B., Venema G., Kok J.;
RT   "Pyrrolidone carboxyl peptidase of Lactococcus lactis MG1363.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-215.
RX   PubMed=10650223; DOI=10.1111/j.1574-6968.2000.tb08954.x;
RA   Curley P., van Sinderen D.;
RT   "Identification and characterisation of a gene encoding aminoacylase
RT   activity from Lactococcus lactis MG1363.";
RL   FEMS Microbiol. Lett. 183:177-182(2000).
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}.
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DR   EMBL; AJ223960; CAA11691.1; -; Genomic_DNA.
DR   EMBL; AJ223962; CAA11699.1; -; Genomic_DNA.
DR   EMBL; AF323462; AAK20299.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97264.1; -; Genomic_DNA.
DR   EMBL; AF168363; AAF36226.1; -; Genomic_DNA.
DR   RefSeq; WP_011834666.1; NZ_WJVF01000051.1.
DR   AlphaFoldDB; O87765; -.
DR   SMR; O87765; -.
DR   STRING; 416870.llmg_0663; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; CAL97264; CAL97264; llmg_0663.
DR   KEGG; llm:llmg_0663; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; KLAYNHK; -.
DR   PhylomeDB; O87765; -.
DR   BioCyc; LLAC416870:LLMG_RS03455-MON; -.
DR   Proteomes; UP000000364; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184722"
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;  23519 MW;  70AE7E36E0882289 CRC64;
     MKILVTGFDP FGDDKINPAI EAVKRLPDEI AGAQIVKLEI PTKFNVSADV VKDAIAKEKP
     DYVLSIGQAG GRFELTPERV AINLDDGRIQ DNAGYQPLNH TIHGDDENAY FTQLPIKAMA
     KAIREAGVPS AVSNTAGTYV CNHIFYQVQY MRDKMFPDIK AGFMHIPFLP EQVVTRPETP
     ALSLDDDVLG ITAAIKAIVS RDGKGDIETI EGKDH