PCP_PYRFU
ID PCP_PYRFU Reviewed; 208 AA.
AC O73944;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=PF1299;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE.
RX PubMed=9756623; DOI=10.1093/oxfordjournals.jbchem.a022179;
RA Tsunasawa S., Nakura S., Tanigawa T., Kato I.;
RT "Pyrrolidone carboxyl peptidase from the hyperthermophilic Archaeon
RT Pyrococcus furiosus: cloning and overexpression in Escherichia coli of the
RT gene, and its application to protein sequence analysis.";
RL J. Biochem. 124:778-783(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=11389725; DOI=10.1046/j.1432-1327.2001.02220.x;
RA Ogasahara K., Khechinashvili N.N., Nakamura M., Yoshimoto T., Yutani K.;
RT "Thermal stability of pyrrolidone carboxyl peptidases from the
RT hyperthermophilic Archaeon, Pyrococcus furiosus.";
RL Eur. J. Biochem. 268:3233-3242(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11432786; DOI=10.1093/oxfordjournals.jbchem.a002948;
RA Tanaka H., Chinami M., Mizushima T., Ogasahara K., Ota M., Tsukihara T.,
RA Yutani K.;
RT "X-ray crystalline structures of pyrrolidone carboxyl peptidase from a
RT hyperthermophile, Pyrococcus furiosus, and its Cys-free mutant.";
RL J. Biochem. 130:107-118(2001).
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 made of two disulfide-linked dimers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR EMBL; AB015291; BAA32989.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81423.1; -; Genomic_DNA.
DR PIR; JE0314; JE0314.
DR RefSeq; WP_011012443.1; NC_018092.1.
DR PDB; 1IOF; X-ray; 2.20 A; A/B/C/D=1-208.
DR PDB; 1IOI; X-ray; 2.70 A; A/B/C/D=1-208.
DR PDB; 1X10; X-ray; 2.00 A; A/B/C/D=1-208.
DR PDB; 1X12; X-ray; 2.00 A; A/B/C/D=1-208.
DR PDB; 1Z8T; X-ray; 2.50 A; A/B/C/D=1-208.
DR PDB; 1Z8W; X-ray; 2.00 A; A/B/C/D=1-208.
DR PDB; 1Z8X; X-ray; 2.00 A; A/B/C/D=1-208.
DR PDB; 2DF5; X-ray; 2.30 A; A/B/C/D=1-204.
DR PDB; 2EO8; X-ray; 2.30 A; A/B/C/D=1-208.
DR PDBsum; 1IOF; -.
DR PDBsum; 1IOI; -.
DR PDBsum; 1X10; -.
DR PDBsum; 1X12; -.
DR PDBsum; 1Z8T; -.
DR PDBsum; 1Z8W; -.
DR PDBsum; 1Z8X; -.
DR PDBsum; 2DF5; -.
DR PDBsum; 2EO8; -.
DR AlphaFoldDB; O73944; -.
DR BMRB; O73944; -.
DR SMR; O73944; -.
DR STRING; 186497.PF1299; -.
DR MEROPS; C15.001; -.
DR PRIDE; O73944; -.
DR EnsemblBacteria; AAL81423; AAL81423; PF1299.
DR GeneID; 41713103; -.
DR KEGG; pfu:PF1299; -.
DR PATRIC; fig|186497.12.peg.1362; -.
DR eggNOG; arCOG05850; Archaea.
DR HOGENOM; CLU_043960_4_0_2; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 97570at2157; -.
DR PhylomeDB; O73944; -.
DR BRENDA; 3.4.19.3; 5243.
DR EvolutionaryTrace; O73944; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..208
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_0000184755"
FT ACT_SITE 79
FT ACT_SITE 142
FT ACT_SITE 166
FT DISULFID 188
FT /note="Interchain"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2EO8"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:1X10"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:1X10"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:1X10"
SQ SEQUENCE 208 AA; 22822 MW; 8977C19E55183BD2 CRC64;
MKVLVTGFEP FGGEKINPTE RIAKDLDGIK IGDAQVFGRV LPVVFGKAKE VLEKTLEEIK
PDIAIHVGLA PGRSAISIER IAVNAIDARI PDNEGKKIED EPIVPGAPTA YFSTLPIKKI
MKKLHERGIP AYISNSAGLY LCNYVMYLSL HHSATKGYPK MSGFIHVPYI PEQIIDKIGK
GQVPPSMCYE MELEAVKVAI EVALEELL
