ID A0A430AQ74_9ENTE Unreviewed; 215 AA.
AC A0A430AQ74;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
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=CBF27_11035 {ECO:0000313|EMBL:RSU10272.1};
OS Vagococcus acidifermentans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Vagococcus.
OX NCBI_TaxID=564710 {ECO:0000313|EMBL:RSU10272.1, ECO:0000313|Proteomes:UP000286773};
RN [1] {ECO:0000313|EMBL:RSU10272.1, ECO:0000313|Proteomes:UP000286773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24798 {ECO:0000313|EMBL:RSU10272.1,
RC ECO:0000313|Proteomes:UP000286773};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU10272.1}.
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DR EMBL; NGKC01000013; RSU10272.1; -; Genomic_DNA.
DR RefSeq; WP_126814368.1; NZ_NGKC01000013.1.
DR AlphaFoldDB; A0A430AQ74; -.
DR OrthoDB; 9779738at2; -.
DR Proteomes; UP000286773; 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 FunFam; 3.40.630.20:FF:000001; Pyrrolidone-carboxylate peptidase; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000286773};
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; 23191 MW; 80187C7B46EB1002 CRC64;
MKILVTGFDP FGTDVTNPAI EAVKRLPDTI SGAEIIKLEI PTVFGKSAAV VREALAEHKP
EYLLCIGQAG GRFGLTPERV AINVDDARIA DNDGNQPIDE AIQETGAPAY FSQHPVKAMV
TAMQKAGLPA AVSNTAGTFV CNHIMYQSLY LTHTSFPETR AGFMHVPFLP EQVTQRPETA
SMSLDDIVRG IRVSLETIIA FDGKEDLKVV GGETH
//
