ID   PCP_DEIRA               Reviewed;         218 AA.
AC   Q9RX25;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=DR_0490;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; AE000513; AAF10067.1; -; Genomic_DNA.
DR   PIR; E75512; E75512.
DR   RefSeq; NP_294213.1; NC_001263.1.
DR   RefSeq; WP_010887135.1; NZ_JMLF01000001.1.
DR   PDB; 5Z40; X-ray; 1.84 A; A/B=1-218.
DR   PDB; 5Z47; X-ray; 1.70 A; A/B=1-218.
DR   PDB; 5Z48; X-ray; 1.55 A; A/B=1-218.
DR   PDBsum; 5Z40; -.
DR   PDBsum; 5Z47; -.
DR   PDBsum; 5Z48; -.
DR   AlphaFoldDB; Q9RX25; -.
DR   SMR; Q9RX25; -.
DR   STRING; 243230.DR_0490; -.
DR   MEROPS; C15.001; -.
DR   PaxDb; 243230-DR_0490; -.
DR   EnsemblBacteria; AAF10067; AAF10067; DR_0490.
DR   GeneID; 69516725; -.
DR   KEGG; dra:DR_0490; -.
DR   PATRIC; fig|243230.17.peg.668; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_3_0; -.
DR   InParanoid; Q9RX25; -.
DR   OrthoDB; 9779738at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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; Peptidase C15, pyroglutamyl peptidase I-like; 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; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; RE07960P; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 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; Reference proteome;
KW   Thiol protease.
FT   CHAIN           1..218
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184716"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           19..27
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           47..61
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           143..157
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           174..179
FT                   /evidence="ECO:0007829|PDB:5Z48"
FT   HELIX           192..209
FT                   /evidence="ECO:0007829|PDB:5Z48"
SQ   SEQUENCE   218 AA;  23096 MW;  5BEB0FFF2F6ACEA4 CRC64;
     MPTLLLTGFE PFHTHPDNPS AQAAQELHGL ELPGGWGVHS ALLPVEPHAA GAALTRLLSE
     QDPGAVLLTG LAAGRPQVTL ERVGVGVMDF QIPDNAGQTY RDQPIEPDAP AAYLATLPLR
     AILAAWREAE IPGDISNSAG LYVCNFVLYH ALHWLREHGR GAVPCGFLHV PANAAVALAV
     PADRPPLPYL PQSEITRAVR VAAEAITAQS SVLQMGKM
//