PCP_PYRAB
ID PCP_PYRAB Reviewed; 200 AA.
AC Q9UYQ9; G8ZIL1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pyrrolidone-carboxylate peptidase;
DE EC=3.4.19.3;
DE AltName: Full=5-oxoprolyl-peptidase;
DE AltName: Full=Pyroglutamyl-peptidase I;
DE Short=PGP-I;
DE Short=Pyrase;
GN Name=pcp; OrderedLocusNames=PYRAB14480; ORFNames=PAB1419;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline.
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;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ248287; CAB50353.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70894.1; -; Genomic_DNA.
DR PIR; D75057; D75057.
DR RefSeq; WP_010868563.1; NC_000868.1.
DR AlphaFoldDB; Q9UYQ9; -.
DR SMR; Q9UYQ9; -.
DR STRING; 272844.PAB1419; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; CAB50353; CAB50353; PAB1419.
DR GeneID; 1495723; -.
DR KEGG; pab:PAB1419; -.
DR PATRIC; fig|272844.11.peg.1539; -.
DR eggNOG; arCOG05850; Archaea.
DR HOGENOM; CLU_043960_4_0_2; -.
DR OMA; HHIATRA; -.
DR OrthoDB; 97570at2157; -.
DR PhylomeDB; Q9UYQ9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
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 Gene3D; 3.40.630.20; -; 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 PANTHER; PTHR23402; PTHR23402; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; SSF53182; 1.
DR TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Thiol protease.
FT CHAIN 1..200
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_0000184754"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /evidence="ECO:0000250"
SQ SEQUENCE 200 AA; 22082 MW; 6F97DB87529D222A CRC64;
MKVLVTGFEP FGGDDKNPTM EIVKFLDGKE IGGAKVIGRV LPVSFKRARK ELVAILDEIK
PDVTINLGLA PGRTHISVER VAVNIIDARI PDNDGEKPID EPIVENGPAA YFATIPTREI
VEEMKRNNIP AVLSYTAGTY LCNFVMYLTL HHSATKGYPR KAGFIHVPYT PDQVIEKKNT
PSMSLELEIK GVEIAIRKSL