PCP1_PHOLL
ID PCP1_PHOLL Reviewed; 220 AA.
AC Q7MAZ1;
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 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=plu4303;
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; CAE16675.1; -; Genomic_DNA.
DR RefSeq; WP_011148398.1; NC_005126.1.
DR AlphaFoldDB; Q7MAZ1; -.
DR SMR; Q7MAZ1; -.
DR STRING; 243265.plu4303; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; CAE16675; CAE16675; plu4303.
DR GeneID; 24169251; -.
DR KEGG; plu:plu4303; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_6; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 1927224at2; -.
DR BioCyc; PLUM243265:PLU_RS21265-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..220
FT /note="Pyrrolidone-carboxylate peptidase 1"
FT /id="PRO_0000184726"
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 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ SEQUENCE 220 AA; 23459 MW; D4A995B3A4A6EFE4 CRC64;
MKTVLITAFE PFDGEAINPS WESVRQLQNQ QLSGAHIETR QLPCVFNTSL TCLYAAIDEI
QPELVIAVGQ AGGRPDITVE RIAININDAR IPDNQGNQPI DTPIVATGPA AYFSTLPIKA
IVSGLQTAGV PASISQSAGT YICNHVMYGL LHHLALTYPK VRGGLVRGGF IHIPYLPEQA
VKHPGTPSMA LETITMALKI AINQALENSG DIAISGGMTH