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Entry: A0A927IW69_9BACI
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ID   A0A927IW69_9BACI        Unreviewed;       200 AA.
AC   A0A927IW69;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 7.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000256|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000256|HAMAP-Rule:MF_00417};
DE            Short=PGP-I {ECO:0000256|HAMAP-Rule:MF_00417};
DE            Short=Pyrase {ECO:0000256|HAMAP-Rule:MF_00417};
GN   Name=pcp {ECO:0000256|HAMAP-Rule:MF_00417,
GN   ECO:0000313|EMBL:MBD8069469.1};
GN   ORFNames=F7888_10780 {ECO:0000313|EMBL:MBD8069469.1};
OS   Bacillus sp. PS06.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2764176 {ECO:0000313|EMBL:MBD8069469.1, ECO:0000313|Proteomes:UP000615181};
RN   [1] {ECO:0000313|EMBL:MBD8069469.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PS06 {ECO:0000313|EMBL:MBD8069469.1};
RA   Bao Z.;
RT   "Draft Genome Sequence of Bacillus pratensis strain PS06.";
RL   Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000256|ARBA:ARBA00002280,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001770,
CC         ECO:0000256|HAMAP-Rule:MF_00417, ECO:0000256|PROSITE-
CC         ProRule:PRU10076};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00417}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family.
CC       {ECO:0000256|ARBA:ARBA00006641, ECO:0000256|HAMAP-Rule:MF_00417}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBD8069469.1}.
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DR   EMBL; JACYHA010000007; MBD8069469.1; -; Genomic_DNA.
DR   RefSeq; WP_191779293.1; NZ_JACYHA010000007.1.
DR   Proteomes; UP000615181; Unassembled WGS sequence.
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; IPR033693; PGPEP1_Glu_AS.
DR   NCBIfam; NF009676; PRK13197.1; 1.
DR   NCBIfam; TIGR00504; pyro_pdase; 1.
DR   PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; PYROGLUTAMYL-PEPTIDASE I; 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; PS01333; PYRASE_GLU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00417};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00417};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000615181};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|HAMAP-
KW   Rule:MF_00417}.
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT                   ECO:0000256|PROSITE-ProRule:PRU10076"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   200 AA;  21720 MW;  D7FE3F36ED3415E1 CRC64;
     MKTLLLTGFV PFLDNPINPT EVIVKALDGQ TLGHYQVVSR VLPVDFSESA VKLEQYMDEV
     EPDVVISLGL AAGRTKITPE RIAINCRDGA ADNQGVKLQD APIAEDGPAG YFSTLPIRAF
     VDALNEANYP ATISNTAGTY LCNNVMYAAL RKIERDGTKI RAGFVHIPAS HELAVQNPKL
     PSWSSRDLEE AIATIIKVLD
//
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