ID A0A087DJT8_9BIFI Unreviewed; 226 AA.
AC A0A087DJT8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10077};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10077};
GN ORFNames=BSCA_1083 {ECO:0000313|EMBL:KFI95788.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI95788.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI95788.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI95788.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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|PROSITE-ProRule:PRU10077};
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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:KFI95788.1}.
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DR EMBL; JGZO01000001; KFI95788.1; -; Genomic_DNA.
DR RefSeq; WP_033516657.1; NZ_JULC01000008.1.
DR AlphaFoldDB; A0A087DJT8; -.
DR STRING; 158787.BSCA_1083; -.
DR GeneID; 85164999; -.
DR eggNOG; COG2039; Bacteria.
DR OrthoDB; 9779738at2; -.
DR Proteomes; UP000029033; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
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 InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
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 SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI95788.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
SQ SEQUENCE 226 AA; 24418 MW; A6F7DBB9CCC13AA5 CRC64;
MQQFNVVISG FERYPGVEVN PAVEVPRALA EQGLGAVAGD FEDPLADVRV NIHAVSLPIS
FANAWPALRD AIEAARPDIV IATGLKHDAR GVMLERCATN LMDAAKPDAD NATPRRVPID
PSGPAAYWTR LPLRSILADF TRDGIPSTLS SDAGTFVCNS LFYSLLNWTA TQDHVLSGFV
SFPPVCEDRK AQRGLPLSQL VAAGRDVVRE TVRYHRSPSS GEILIA
//
