PCP1_CALS4
ID PCP1_CALS4 Reviewed; 203 AA.
AC Q8RBX8;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pyrrolidone-carboxylate peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp1 {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=TTE0678;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM23942.1; -; Genomic_DNA.
DR RefSeq; WP_011025084.1; NC_003869.1.
DR AlphaFoldDB; Q8RBX8; -.
DR SMR; Q8RBX8; -.
DR STRING; 273068.TTE0678; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; AAM23942; AAM23942; TTE0678.
DR KEGG; tte:TTE0678; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_9; -.
DR OMA; HHIATRA; -.
DR OrthoDB; 1927224at2; -.
DR Proteomes; UP000000555; 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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..203
FT /note="Pyrrolidone-carboxylate peptidase 1"
FT /id="PRO_0000184746"
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 203 AA; 22307 MW; ACB72948C5B8BC72 CRC64;
MKILVTAFDP FGGESVNPSY EVLKNLKDNI EGAEIIKLQV PTAFYVSVEK AIEKIKEVNP
DAVLSIGQAG GRYDISVERV AINIDDARIP DNMGQQPIDI PIDPEGPPAY FATIPIKEIV
EAIKKENLPA SVSNSAGTYV CNHLMYGILN YIHKNKLNIK AGFIHIPYLP EQVLEKPNTP
YMSLSDMVKA IETAIKVIVK AMA
