PCP2_RALSO
ID PCP2_RALSO Reviewed; 215 AA.
AC Q8XT56;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyrrolidone-carboxylate peptidase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp2 {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=RSp0259;
GN ORFNames=RS03707;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
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; AL646053; CAD17410.1; -; Genomic_DNA.
DR RefSeq; WP_011003573.1; NC_003296.1.
DR AlphaFoldDB; Q8XT56; -.
DR SMR; Q8XT56; -.
DR STRING; 267608.RSp0259; -.
DR MEROPS; C15.001; -.
DR PRIDE; Q8XT56; -.
DR EnsemblBacteria; CAD17410; CAD17410; RSp0259.
DR GeneID; 60503196; -.
DR KEGG; rso:RSp0259; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_4; -.
DR OMA; HHIATRA; -.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Protease; Reference proteome;
KW Thiol protease.
FT CHAIN 1..215
FT /note="Pyrrolidone-carboxylate peptidase 2"
FT /id="PRO_0000184730"
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; 22628 MW; 68B1D63048C3BA57 CRC64;
MTTVLITGIE PFESDPTNPS WDIARALDGE RIDGATLVAR QLPCVFGRAN RELVAAIEAT
QPSLVLALGL ASGRSELSVE RVAINVIDAR IPDNAGNQPV DVPVVADGPA AYFSSLPIKA
IVHALRAAGV PAAVSQSAGT YNCNHLFYGL MHHIATRAPR MRGGFIHVPA TPELAARHPG
RPSLRLDAQI AGMRVAVRTA LATQGDLRLS GGTLH