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Database: UniProt
Entry: I7LGK8_9LACO
LinkDB: I7LGK8_9LACO
Original site: I7LGK8_9LACO 
ID   I7LGK8_9LACO            Unreviewed;       215 AA.
AC   I7LGK8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
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   ORFNames=BN52_00065 {ECO:0000313|EMBL:CCI87738.1};
OS   Lactobacillus gigeriorum DSM 23908 = CRBIP 24.85.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423751 {ECO:0000313|EMBL:CCI87738.1, ECO:0000313|Proteomes:UP000009326};
RN   [1] {ECO:0000313|EMBL:CCI87738.1, ECO:0000313|Proteomes:UP000009326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRBIP 24.85T {ECO:0000313|Proteomes:UP000009326};
RA   Cousin S., Ma L., Creno S., Clermont D., Loux V., Bizet C., Bouchier C.;
RT   "Draft genome sequence of Lactobacillus gigeriorum CRBIP 24.85T, isolated
RT   from chicken crop.";
RL   Submitted (JUN-2012) 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:CCI87738.1}.
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DR   EMBL; CAKC01000090; CCI87738.1; -; Genomic_DNA.
DR   RefSeq; WP_008474048.1; NZ_CAKC01000090.1.
DR   AlphaFoldDB; I7LGK8; -.
DR   STRING; 1423751.FC38_GL001543; -.
DR   MEROPS; C15.001; -.
DR   PATRIC; fig|1423751.3.peg.1592; -.
DR   OrthoDB; 9779738at2; -.
DR   Proteomes; UP000009326; 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; 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 {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   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|HAMAP-
KW   Rule:MF_00417}.
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT                   ECO:0000256|PROSITE-ProRule:PRU10076"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT                   ECO:0000256|PROSITE-ProRule:PRU10077"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   215 AA;  23426 MW;  A2E8F8B63422D57B CRC64;
     MKILVTGFDP FGGEKINPAI EAVKLLPDTI AGAEIRKLEI PTVFDKSAQV VHEAIAEFKP
     DYVLNVGQAG GRAELTPEKV AINYDDGRIA DNEGFQPMNR TIHEDGETAY FTQLPIKAMV
     RAIREVGVPA RVSTTAGTYV CNHIMYQVQY MRDKEFTDIK AGFIHIPFLP SQVVDKPGMP
     SMSLEDIVKG LTAAIEAIVA YDGKADAETI EGSIA
//
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