PCP_THELN
ID PCP_THELN Reviewed; 220 AA.
AC O07883; H3ZQF6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pyrrolidone-carboxylate peptidase;
DE EC=3.4.19.3;
DE AltName: Full=5-oxoprolyl-peptidase;
DE AltName: Full=Pyroglutamyl-peptidase I;
DE Short=PGP-I;
GN Name=pcp; ORFNames=OCC_03923;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=11057915; DOI=10.1007/s007920070017;
RA Singleton M.R., Taylor S.J.C., Parrat J.S., Littlechild J.A.;
RT "Cloning, expression, and characterization of pyrrolidone carboxyl
RT peptidase from the archaeon Thermococcus litoralis.";
RL Extremophiles 4:297-303(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=10089475; DOI=10.1107/s0907444998016035;
RA Singleton M.R., Isupov M.N., Littlechild J.A.;
RT "Crystallization and preliminary X-ray diffraction studies of pyrrolidone
RT carboxyl peptidase from the hyperthermophilic archaeon Thermococcus
RT litoralis.";
RL Acta Crystallogr. D 55:702-703(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS).
RX PubMed=10368293; DOI=10.1016/s0969-2126(99)80034-3;
RA Singleton M.R., Isupov M.N., Littlechild J.A.;
RT "X-ray structure of pyrrolidone carboxyl peptidase from the
RT hyperthermophilic archaeon Thermococcus litoralis.";
RL Structure 7:237-244(1999).
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR EMBL; Y13966; CAA74299.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR78169.1; -; Genomic_DNA.
DR RefSeq; WP_004068885.1; NC_022084.1.
DR PDB; 1A2Z; X-ray; 1.73 A; A/B/C/D=1-220.
DR PDBsum; 1A2Z; -.
DR AlphaFoldDB; O07883; -.
DR SMR; O07883; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; EHR78169; EHR78169; OCC_03923.
DR GeneID; 16550208; -.
DR KEGG; tlt:OCC_03923; -.
DR HOGENOM; CLU_043960_4_0_2; -.
DR OMA; HHIATRA; -.
DR OrthoDB; 97570at2157; -.
DR BRENDA; 3.4.19.3; 6302.
DR EvolutionaryTrace; O07883; -.
DR Proteomes; UP000015502; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Hydrolase; Protease;
KW Thiol protease.
FT CHAIN 1..220
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_0000184760"
FT ACT_SITE 80
FT ACT_SITE 143
FT ACT_SITE 167
FT DISULFID 190
FT /note="Interchain"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1A2Z"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1A2Z"
FT HELIX 191..210
FT /evidence="ECO:0007829|PDB:1A2Z"
SQ SEQUENCE 220 AA; 24747 MW; 58B9774015D07ADC CRC64;
MKKVLITGFE PFGGDSKNPT EQIAKYFDRK QIGNAMVYGR VLPVSVKRAT IELKRYLEEI
KPEIVINLGL APTYSNITVE RIAVNIIDAR IPDNDGYQPI DEKIEEDAPL AYMATLPVRA
ITKTLRDNGI PATISYSAGT YLCNYVMFKT LHFSKIEGYP LKAGFIHVPY TPDQVVNKFF
LLGKNTPSMC LEAEIKAIEL AVKVSLDYLE KDRDDIKIPL
