PCP1_RALSO
ID PCP1_RALSO Reviewed; 215 AA.
AC Q8XXE9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Pyrrolidone-carboxylate peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp1 {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=RSc2165;
GN ORFNames=RS01434;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD15872.1; -; Genomic_DNA.
DR RefSeq; WP_011002094.1; NC_003295.1.
DR AlphaFoldDB; Q8XXE9; -.
DR SMR; Q8XXE9; -.
DR STRING; 267608.RSc2165; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; CAD15872; CAD15872; RSc2165.
DR GeneID; 60501677; -.
DR KEGG; rso:RSc2165; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_4; -.
DR OMA; KLAYNHK; -.
DR Proteomes; UP000001436; 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 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.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..215
FT /note="Pyrrolidone-carboxylate peptidase 1"
FT /id="PRO_0000184729"
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; 22780 MW; 02CAC31365F93D12 CRC64;
MPTVLVTGFD PFENEPVNPS WEAVRTLDGQ GIAGADIVTR QLPTVFGESI RVLDRLLMSL
RPDVVIAVGQ AGGRAEMAIE RVAINVDDAR IADNAGRQPI DTAIVAGGPA AYFSTLPIKA
IVHELRAAGV PASVSQTAGT FVCNHVFYGL MHAIAHHGLH ARGGFIHIPY LPAQAAGHPG
QPSMAHDTVV AGLRIAIETT LRRQEDIREA GGQLH
