PCP_PYRHO
ID PCP_PYRHO Reviewed; 206 AA.
AC O58321;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=PH0596;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=12836705; DOI=10.1023/a:1021257701676;
RA Sokabe M., Kawamura T., Sakai N., Yao M., Watanabe N., Tanaka I.;
RT "The X-ray crystal structure of pyrrolidone-carboxylate peptidase from
RT hyperthermophilic archaea Pyrococcus horikoshii.";
RL J. Struct. Funct. Genomics 2:145-154(2002).
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}.
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DR EMBL; BA000001; BAA29685.1; -; Genomic_DNA.
DR PIR; H71174; H71174.
DR PDB; 1IU8; X-ray; 1.60 A; A/B=1-206.
DR PDBsum; 1IU8; -.
DR AlphaFoldDB; O58321; -.
DR SMR; O58321; -.
DR MINT; O58321; -.
DR STRING; 70601.3257002; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; BAA29685; BAA29685; BAA29685.
DR KEGG; pho:PH0596; -.
DR eggNOG; arCOG05850; Archaea.
DR OMA; KLAYNHK; -.
DR BRENDA; 3.4.19.3; 5244.
DR EvolutionaryTrace; O58321; -.
DR Proteomes; UP000000752; 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; Hydrolase; Protease; Thiol protease.
FT CHAIN 1..206
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_0000184756"
FT ACT_SITE 76
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:1IU8"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1IU8"
FT HELIX 182..202
FT /evidence="ECO:0007829|PDB:1IU8"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1IU8"
SQ SEQUENCE 206 AA; 22640 MW; CA16F1009BDB1766 CRC64;
MKILLTGFEP FGGDDKNPTM DIVEALSERI PEVVGEILPV SFKRAREKLL KVLDDVRPDI
TINLGLAPGR THISVERVAV NMIDARIPDN DGEQPKDEPI VEGGPAAYFA TIPTREIVEE
MKKNGIPAVL SYTAGTYLCN FAMYLTLHTS ATKGYPKIAG FIHVPYTPDQ VLEKKNTPSM
SLDLEIKGVE IAIRVAQSAL HSSQLR
