PCP_MYCTA
ID PCP_MYCTA Reviewed; 222 AA.
AC A5TZ46;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=MRA_0328;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ72046.1; -; Genomic_DNA.
DR RefSeq; WP_003401632.1; NZ_CP016972.1.
DR AlphaFoldDB; A5TZ46; -.
DR SMR; A5TZ46; -.
DR STRING; 419947.MRA_0328; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; ABQ72046; ABQ72046; MRA_0328.
DR GeneID; 45424287; -.
DR KEGG; mra:MRA_0328; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_3_11; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 1927224at2; -.
DR Proteomes; UP000001988; 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; Thiol protease.
FT CHAIN 1..222
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_1000050134"
FT ACT_SITE 80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ SEQUENCE 222 AA; 23193 MW; C542D9FD2CE2477D CRC64;
MSKVLVTGFG PYGVTPVNPA QLTAEELDGR TIAGATVISR IVPNTFFESI AAAQQAIAEI
EPALVIMLGE YPGRSMITVE RLAQNVNDCG RYGLADCAGR VLVGEPTDPA GPVAYHATVP
VRAMVLAMRK AGVPADVSDA AGTFVCNHLM YGVLHHLAQK GLPVRAGWIH LPCLPSVAAL
DHNLGVPSMS VQTAVAGVTA GIEAAIRQSA DIREPIPSRL QI
