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PCP_BACCN
ID   PCP_BACCN               Reviewed;         215 AA.
AC   A7GQB6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN   Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=Bcer98_2056;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00417};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00417}.
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DR   EMBL; CP000764; ABS22324.1; -; Genomic_DNA.
DR   RefSeq; WP_012094517.1; NC_009674.1.
DR   AlphaFoldDB; A7GQB6; -.
DR   SMR; A7GQB6; -.
DR   STRING; 315749.Bcer98_2056; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; ABS22324; ABS22324; Bcer98_2056.
DR   GeneID; 56417620; -.
DR   KEGG; bcy:Bcer98_2056; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; KLAYNHK; -.
DR   OrthoDB; 1927224at2; -.
DR   Proteomes; UP000002300; 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..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_1000080514"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   215 AA;  23613 MW;  E6B0DBAB6897F75A CRC64;
     MKTVLLTGFD PFGGEKINPA WEVAKALHEK EGNGYKVISK QIPTVFHKSI EQLESYIDEF
     NPELIICIGQ AGGRADITVE RVAINVDDAR IPDNENYQPI DVPIIEDGPV AYWSTLPIKA
     IVKKLREEGI PASVSQTAGT FVCNHLFYGL MHRLAIKNKS TRGGFVHIPF LPEQASLHAN
     QPSMSLSTII AGIQLLIEVA LQVEKDIVEC GGTTH
 
 
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