ID   PCP_THEM4               Reviewed;         202 AA.
AC   A6LL24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Tmel_0762;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000716; ABR30625.1; -; Genomic_DNA.
DR   RefSeq; WP_012056986.1; NC_009616.1.
DR   AlphaFoldDB; A6LL24; -.
DR   SMR; A6LL24; -.
DR   STRING; 391009.Tmel_0762; -.
DR   MEROPS; C15.001; -.
DR   KEGG; tme:Tmel_0762; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_0_0; -.
DR   OrthoDB; 9779738at2; -.
DR   Proteomes; UP000001110; 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; Peptidase C15, pyroglutamyl peptidase I-like; 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   NCBIfam; TIGR00504; pyro_pdase; 1.
DR   PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; RE07960P; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 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..202
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_1000050152"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   202 AA;  22533 MW;  F0AC5399517FA926 CRC64;
     MKVLVTGFEP FNGETINPSF EAIKMLPDEV EGAKIIKAKL PTVFRKSLCE LEELISKENP
     DIVICVGQAA GRSKISIERV AINIDDAEIN DNEGNKPKDE KIFVDGENAY FSNLPIKLMV
     KTIKEHNIPA EISNSAGTYV CNHVFYGLMY LIDKKFKNLK GGFIHVPFSH NQVLEKKNVP
     SMSLEDITNG LFYAIKGVLS EK
//