PCP_YERP3
ID PCP_YERP3 Reviewed; 215 AA.
AC A7FFS3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=YpsIP31758_1120;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS48933.1; -; Genomic_DNA.
DR RefSeq; WP_012104778.1; NC_009708.1.
DR AlphaFoldDB; A7FFS3; -.
DR SMR; A7FFS3; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; ABS48933; ABS48933; YpsIP31758_1120.
DR KEGG; ypi:YpsIP31758_1120; -.
DR HOGENOM; CLU_043960_4_0_6; -.
DR OMA; KLAYNHK; -.
DR Proteomes; UP000002412; 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_1000060081"
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; 23168 MW; 5F19B48F8976B4A5 CRC64;
MRRVLITGFE PFGGERINPS WEVVKQMNDL MMGGVRIVAR QLPCAFGEAL TALNTAIDDV
QPVLVLAIGQ AGGRADITIE RVAINVDDAR IPDNLGNQPV DQPIIQEGPA AYFTRLPIKA
MVQGIREAGI PASVSQTAGT YVCNHVMYGL LHRLNQFNNE VKGGFIHIPY LPEQAVDHPG
APSMSAQSVL VALELAISIA LQIEHDLHIT GGPVH
