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Database: UniProt
Entry: W1X484_9FIRM
LinkDB: W1X484_9FIRM
Original site: W1X484_9FIRM 
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
//
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