ID U2TG48_9ACTN Unreviewed; 210 AA.
AC U2TG48;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10077};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10077};
GN Name=pcp {ECO:0000313|EMBL:ERL12024.1};
GN ORFNames=HMPREF1248_0657 {ECO:0000313|EMBL:ERL12024.1};
OS Coriobacteriaceae bacterium BV3Ac1.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL12024.1, ECO:0000313|Proteomes:UP000016652};
RN [1] {ECO:0000313|EMBL:ERL12024.1, ECO:0000313|Proteomes:UP000016652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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:ERL12024.1}.
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DR EMBL; AWUP01000011; ERL12024.1; -; Genomic_DNA.
DR AlphaFoldDB; U2TG48; -.
DR PATRIC; fig|1111135.3.peg.905; -.
DR eggNOG; COG2039; Bacteria.
DR OrthoDB; 9779738at2; -.
DR Proteomes; UP000016652; 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; IPR029762; PGP-I_bact-type.
DR InterPro; IPR033694; PGPEP1_Cys_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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ERL12024.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000016652};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
SQ SEQUENCE 210 AA; 22916 MW; 5096383BEE8BE864 CRC64;
MKLLLTAFDA FGGDKLNASQ LALDQLPDEI EGVRLQKLFI PTEFQKAPAL IRQTIQELLP
DAVVSLGQAT GRRTLTVERI GVNLIDARIP DNSGNQPKDQ CIVPQGPDAL FSNLPTRQMV
EAMQHVGIPA ELSYTAGTYV CNSVLYSTRY FCLTHYPNIL SGFIHLPATP EQTASHEGNT
EIPSMSTAKV VLGLVEALKA VILYQDSPLQ
//
