PCP1_SACS2
ID PCP1_SACS2 Reviewed; 211 AA.
AC P58201;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Pyrrolidone-carboxylate peptidase 1;
DE EC=3.4.19.3;
DE AltName: Full=5-oxoprolyl-peptidase 1;
DE AltName: Full=Pyroglutamyl-peptidase I 1;
DE Short=PGP-I 1;
DE Short=Pyrase 1;
GN Name=pcp1; OrderedLocusNames=SSO1465;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; 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; AAK41693.1; -; Genomic_DNA.
DR PIR; F90304; F90304.
DR RefSeq; WP_009989153.1; NC_002754.1.
DR AlphaFoldDB; P58201; -.
DR SMR; P58201; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; AAK41693; AAK41693; SSO1465.
DR GeneID; 44130284; -.
DR KEGG; sso:SSO1465; -.
DR PATRIC; fig|273057.12.peg.1497; -.
DR eggNOG; arCOG05850; Archaea.
DR HOGENOM; CLU_043960_4_3_2; -.
DR InParanoid; P58201; -.
DR OMA; KLAYNHK; -.
DR PhylomeDB; P58201; -.
DR Proteomes; UP000001974; 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 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..211
FT /note="Pyrrolidone-carboxylate peptidase 1"
FT /id="PRO_0000184758"
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 211 AA; 23681 MW; 84416BE3CB745AB4 CRC64;
MTVLLFGFEP FLEYKENPSQ LIVEALNRST ILKEEVKGVI LPVEYKKIED VIVTKIRETK
PILTLGIGLA PGRAKITPEK IAINYRYSRE GDNAGKKYRG EKIDPLGQDG IFTNIPVEDL
VDLLNENGIP AELSLSAGSY LCNNAMYIII REARKYNSLG GFIHVPLHES YAARIQRSIP
SMSLDTMIRG IKLSIEFILT NKNKKENLTL S