ID   PCP_BACAM               Reviewed;         215 AA.
AC   P46107;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
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;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-68 AND CYS-144.
RX   PubMed=8095933; DOI=10.1093/oxfordjournals.jbchem.a124005;
RA   Yoshimoto T., Shimoda T., Kitazono A., Kabashima T., Ito K., Tsuru D.;
RT   "Pyroglutamyl peptidase gene from Bacillus amyloliquefaciens: cloning,
RT   sequencing, expression, and crystallization of the expressed enzyme.";
RL   J. Biochem. 113:67-73(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10196127; DOI=10.1016/s0969-2126(99)80053-7;
RA   Odagaki Y., Hayashi A., Okada K., Hirotsu K., Kabashima T., Ito K.,
RA   Yoshimoto T., Tsuru D., Sato M., Clardy J.;
RT   "The crystal structure of pyroglutamyl peptidase I from Bacillus
RT   amyloliquefaciens reveals a new structure for a cysteine protease.";
RL   Structure 7:399-411(1999).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. Stable from pH 7.0 to 9.0.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; D11035; BAA01791.1; -; Genomic_DNA.
DR   PIR; JX0244; JX0244.
DR   RefSeq; WP_013350909.1; NZ_VRTX01000011.1.
DR   PDB; 1AUG; X-ray; 2.00 A; A/B/C/D=1-215.
DR   PDB; 3RNZ; X-ray; 2.01 A; A/B/C/D=1-215.
DR   PDB; 3RO0; X-ray; 1.50 A; A/B/C/D=1-215.
DR   PDBsum; 1AUG; -.
DR   PDBsum; 3RNZ; -.
DR   PDBsum; 3RO0; -.
DR   AlphaFoldDB; P46107; -.
DR   SMR; P46107; -.
DR   STRING; 692420.BAMF_0240; -.
DR   MEROPS; C15.001; -.
DR   eggNOG; COG2039; Bacteria.
DR   OMA; KLAYNHK; -.
DR   EvolutionaryTrace; P46107; -.
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..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184706"
FT   ACT_SITE        81
FT   ACT_SITE        144
FT   ACT_SITE        168
FT   MUTAGEN         68
FT                   /note="C->S: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8095933"
FT   MUTAGEN         144
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8095933"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           20..27
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           49..61
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          77..86
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           143..158
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           173..175
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:3RO0"
FT   HELIX           186..202
FT                   /evidence="ECO:0007829|PDB:3RO0"
SQ   SEQUENCE   215 AA;  23287 MW;  731A9F80733E807C CRC64;
     MEKKVLLTGF DPFGGETVNP SWEAVKRLNG AAEGPASIVS EQVPTVFYKS LAVLREAIKK
     HQPDIIICVG QAGGRMQITP ERVAINLNEA RIPDNEGNQP VGEDISQGGP AAYWTGLPIK
     RIVEEIKKEG IPAAVSYTAG TFVCNHLFYG LMDEISRHHP HIRGGFIHIP YIPEQTLQKS
     APSLSLDHIT KALKIAAVTA AVHEDDIETG GGELH