ID   PCP_MYCTO               Reviewed;         222 AA.
AC   P9WIJ4; L0T508; O07930; P0A5R4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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=MT0334;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44557.1; -; Genomic_DNA.
DR   PIR; H70525; H70525.
DR   RefSeq; WP_003401632.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIJ4; -.
DR   SMR; P9WIJ4; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; AAK44557; AAK44557; MT0334.
DR   GeneID; 45424287; -.
DR   KEGG; mtc:MT0334; -.
DR   PATRIC; fig|83331.31.peg.354; -.
DR   HOGENOM; CLU_043960_4_3_11; -.
DR   Proteomes; UP000001020; 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..222
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000427996"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  23193 MW;  C542D9FD2CE2477D CRC64;
     MSKVLVTGFG PYGVTPVNPA QLTAEELDGR TIAGATVISR IVPNTFFESI AAAQQAIAEI
     EPALVIMLGE YPGRSMITVE RLAQNVNDCG RYGLADCAGR VLVGEPTDPA GPVAYHATVP
     VRAMVLAMRK AGVPADVSDA AGTFVCNHLM YGVLHHLAQK GLPVRAGWIH LPCLPSVAAL
     DHNLGVPSMS VQTAVAGVTA GIEAAIRQSA DIREPIPSRL QI