ID   PCP2_SACS2              Reviewed;         209 AA.
AC   P58202;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 130.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase 2;
DE            EC=3.4.19.3;
DE   AltName: Full=5-oxoprolyl-peptidase 2;
DE   AltName: Full=Pyroglutamyl-peptidase I 2;
DE            Short=PGP-I 2;
DE            Short=Pyrase 2;
GN   Name=pcp2; OrderedLocusNames=SSO1607;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000250}.
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;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006641; AAK41818.1; -; Genomic_DNA.
DR   PIR; C90320; C90320.
DR   RefSeq; WP_010923507.1; NC_002754.1.
DR   AlphaFoldDB; P58202; -.
DR   SMR; P58202; -.
DR   FunCoup; P58202; 49.
DR   MEROPS; C15.001; -.
DR   PaxDb; 273057-SSO1607; -.
DR   EnsemblBacteria; AAK41818; AAK41818; SSO1607.
DR   GeneID; 15297022; -.
DR   KEGG; sso:SSO1607; -.
DR   PATRIC; fig|273057.12.peg.1645; -.
DR   eggNOG; arCOG05850; Archaea.
DR   HOGENOM; CLU_043960_4_3_2; -.
DR   InParanoid; P58202; -.
DR   PhylomeDB; P58202; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00501; Peptidase_C15; 1.
DR   FunFam; 3.40.630.20:FF:000005; Pyrrolidone-carboxylate peptidase; 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; NF009672; PRK13193.1; 1.
DR   PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; PYROGLUTAMYL-PEPTIDASE I; 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; Reference proteome; Thiol protease.
FT   CHAIN           1..209
FT                   /note="Pyrrolidone-carboxylate peptidase 2"
FT                   /id="PRO_0000184759"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  23404 MW;  AAE205344FD024B7 CRC64;
     MTVLLFGFEP FLEYKENPSQ LIVEALNGST ILKEEVKGVI LPVEYEKIED LIVTKIREMK
     PILTLGIGVA PGRAKITPEK IAINYKYSRE GDNAGKKYKG EKIDPLGQDG IFTNIPVEDL
     VDLLNENGIP AELSLSAGSY LCNNAMYIII REARKYNSLG GFIHVPLHES YAARIQRPIP
     SMSLDTMIRG IRLSMEFILT NKKENLTFS
//