PCP2_PHOLL
ID PCP2_PHOLL Reviewed; 218 AA.
AC Q7MZ76;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=plu4418;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571873; CAE16790.1; -; Genomic_DNA.
DR RefSeq; WP_011148508.1; NC_005126.1.
DR AlphaFoldDB; Q7MZ76; -.
DR SMR; Q7MZ76; -.
DR STRING; 243265.plu4418; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; CAE16790; CAE16790; plu4418.
DR GeneID; 24170595; -.
DR KEGG; plu:plu4418; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_6; -.
DR OMA; HHIATRA; -.
DR OrthoDB; 1927224at2; -.
DR BioCyc; PLUM243265:PLU_RS21850-MON; -.
DR Proteomes; UP000002514; 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; Reference proteome; Thiol protease.
FT CHAIN 1..218
FT /note="Pyrrolidone-carboxylate peptidase 2"
FT /id="PRO_0000184727"
FT ACT_SITE 83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ SEQUENCE 218 AA; 23158 MW; 6519209111AB823C CRC64;
MTTQKTVLIT GFEPFGKETI NPSWEAAKQL QGRELCGARV EARQLPCVFD VSLACLYAAI
DDVQPDLVIA VGQAGGRPNI TVERVAININ DASIPDNQGN QPINTPIVAT GPAAYFATLP
INAIVKGLRD AGVPASISQT AGTFVCNHVM YGLLHHLACI YPEIRGGVLH IPYLPEQAAR
YSGTPSMALE TVITALEIAI DEALKNSEDI ANNGDTAH
