PCP_DEIRA
ID PCP_DEIRA Reviewed; 218 AA.
AC Q9RX25;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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;
DE Short=Pyrase;
GN Name=pcp; OrderedLocusNames=DR_0490;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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}.
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DR EMBL; AE000513; AAF10067.1; -; Genomic_DNA.
DR PIR; E75512; E75512.
DR RefSeq; NP_294213.1; NC_001263.1.
DR RefSeq; WP_010887135.1; NZ_CP015081.1.
DR PDB; 5Z40; X-ray; 1.84 A; A/B=1-218.
DR PDB; 5Z47; X-ray; 1.70 A; A/B=1-218.
DR PDB; 5Z48; X-ray; 1.55 A; A/B=1-218.
DR PDBsum; 5Z40; -.
DR PDBsum; 5Z47; -.
DR PDBsum; 5Z48; -.
DR AlphaFoldDB; Q9RX25; -.
DR SMR; Q9RX25; -.
DR STRING; 243230.DR_0490; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; AAF10067; AAF10067; DR_0490.
DR KEGG; dra:DR_0490; -.
DR PATRIC; fig|243230.17.peg.668; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_3_0; -.
DR InParanoid; Q9RX25; -.
DR OMA; HHIATRA; -.
DR OrthoDB; 1927224at2; -.
DR Proteomes; UP000002524; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Thiol protease.
FT CHAIN 1..218
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_0000184716"
FT ACT_SITE 81
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:5Z48"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:5Z48"
FT HELIX 192..209
FT /evidence="ECO:0007829|PDB:5Z48"
SQ SEQUENCE 218 AA; 23096 MW; 5BEB0FFF2F6ACEA4 CRC64;
MPTLLLTGFE PFHTHPDNPS AQAAQELHGL ELPGGWGVHS ALLPVEPHAA GAALTRLLSE
QDPGAVLLTG LAAGRPQVTL ERVGVGVMDF QIPDNAGQTY RDQPIEPDAP AAYLATLPLR
AILAAWREAE IPGDISNSAG LYVCNFVLYH ALHWLREHGR GAVPCGFLHV PANAAVALAV
PADRPPLPYL PQSEITRAVR VAAEAITAQS SVLQMGKM
