ID   PCP_ALKHC               Reviewed;         201 AA.
AC   Q9K6U4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=BH3631;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB07350.1; -; Genomic_DNA.
DR   PIR; G84103; G84103.
DR   RefSeq; WP_010899759.1; NC_002570.2.
DR   AlphaFoldDB; Q9K6U4; -.
DR   SMR; Q9K6U4; -.
DR   STRING; 272558.10176255; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; BAB07350; BAB07350; BAB07350.
DR   KEGG; bha:BH3631; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_3_9; -.
DR   OMA; VVYQKAK; -.
DR   OrthoDB; 1927224at2; -.
DR   Proteomes; UP000001258; 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; Reference proteome; Thiol protease.
FT   CHAIN           1..201
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184711"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22181 MW;  0843388B886A7591 CRC64;
     MGNIILLTGF QPFLDYSINP TEAIVKELNG RKIGEYEVRG VILPVSFRES GDLLLHHFQT
     VQPTAVFMLG LAAGRGKITP ERVAININSG PEDRDGIAPV DEPIRQGGPA AYFSTLPVRR
     LIQRLNEEGF PAEMSNSAGT YVCNHVMYRM LDYLHEKGSE QVAAGFVHLP ASKELAAQHH
     SLPSMDLKDL TRAVTLMIEE L