ID   PCP_BACVZ               Reviewed;         215 AA.
AC   A7Z119;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=RBAM_002960;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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}.
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DR   EMBL; CP000560; ABS72695.1; -; Genomic_DNA.
DR   RefSeq; WP_011996270.1; NC_009725.2.
DR   AlphaFoldDB; A7Z119; -.
DR   SMR; A7Z119; -.
DR   MEROPS; C15.001; -.
DR   KEGG; bay:RBAM_002960; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   Proteomes; UP000001120; 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_1000050121"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   215 AA;  23234 MW;  45CC5A1F6DBED713 CRC64;
     MEKKVLLTGF DPFGGETVNP SWEAVKRLNG AAEGPASIVS EQVPTVFYKS LAVLREAIKK
     HQPDIIICVG QAGGRMQITP ERVAINLNEA RIPDNEGNQP VGENISQGGP AAYWTGLPIK
     RIVEEIKKEG IPAAVSYTAG TFVCNHLFYG LMDEITRHHP HIRGGFIHIP YIPEQTLQKS
     APSLSLDLVT KALKIAAVTA AAHEDDIETG GGELH
//