ID W1X484_9FIRM Unreviewed; 138 AA.
AC W1X484;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 03-MAY-2023, entry version 39.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10076};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10076};
DE Flags: Fragment;
GN ORFNames=Q620_VSAC00052G0001 {ECO:0000313|EMBL:ETJ23534.1};
OS Veillonella sp. DORA_A_3_16_22.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1403932 {ECO:0000313|EMBL:ETJ23534.1, ECO:0000313|Proteomes:UP000050220};
RN [1] {ECO:0000313|EMBL:ETJ23534.1, ECO:0000313|Proteomes:UP000050220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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 -!- 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|PROSITE-ProRule:PRU10076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:ETJ23534.1}.
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DR EMBL; AZMK01000052; ETJ23534.1; -; Genomic_DNA.
DR AlphaFoldDB; W1X484; -.
DR Proteomes; UP000050220; 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; IPR033693; PGPEP1_Glu_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 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10076"
FT NON_TER 138
FT /evidence="ECO:0000313|EMBL:ETJ23534.1"
SQ SEQUENCE 138 AA; 14827 MW; DEB0C849F7411E3E CRC64;
MKTILITGFD PFGGEPINPA WEAVKTMDGY TDGDYKVVTQ MVPTVRYKSV DTVKAAAEQC
QPDFILCVGQ AGGRPDITVE RVAINCDDFR IPDNGGNQPE DEPVVSDGPS AYFATLPIKN
IVNALHQNGI PAKVSNTA
//