ID E8URW2_THEBF Unreviewed; 205 AA.
AC E8URW2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000256|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase {ECO:0000256|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I {ECO:0000256|HAMAP-Rule:MF_00417};
DE Short=PGP-I {ECO:0000256|HAMAP-Rule:MF_00417};
DE Short=Pyrase {ECO:0000256|HAMAP-Rule:MF_00417};
GN Name=pcp {ECO:0000256|HAMAP-Rule:MF_00417};
GN OrderedLocusNames=Thebr_0982 {ECO:0000313|EMBL:ADV79559.1};
OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS AKO-1) (Thermoanaerobacter finnii).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79559.1, ECO:0000313|Proteomes:UP000002062};
RN [1] {ECO:0000313|EMBL:ADV79559.1, ECO:0000313|Proteomes:UP000002062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC {ECO:0000313|Proteomes:UP000002062};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000256|ARBA:ARBA00002280,
CC ECO:0000256|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:0000256|ARBA:ARBA00001770,
CC ECO:0000256|HAMAP-Rule:MF_00417, ECO:0000256|PROSITE-
CC ProRule:PRU10076};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00417}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641, ECO:0000256|HAMAP-Rule:MF_00417}.
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DR EMBL; CP002466; ADV79559.1; -; Genomic_DNA.
DR AlphaFoldDB; E8URW2; -.
DR MEROPS; C15.001; -.
DR KEGG; tbo:Thebr_0982; -.
DR HOGENOM; CLU_043960_4_0_9; -.
DR Proteomes; UP000002062; 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; Peptidase C15, pyroglutamyl peptidase I-like; 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 NCBIfam; TIGR00504; pyro_pdase; 1.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF1; RE07960P; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00417};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00417};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00417};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|HAMAP-
KW Rule:MF_00417}.
FT ACT_SITE 80
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT ECO:0000256|PROSITE-ProRule:PRU10076"
FT ACT_SITE 143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT ECO:0000256|PROSITE-ProRule:PRU10077"
FT ACT_SITE 167
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00417"
SQ SEQUENCE 205 AA; 22601 MW; B824C42AD865F3CE CRC64;
MIMKILVTAF DPFGGENINP SYEVLKNLKD NIEGAEIIKI QVPTVFYLSV EKVIEKIKEV
KPDAVLSIGQ AGGRYDITVE RIAINIDDAR IPDNIGQQPI DTPIDPEGAP AYFATIPIKE
IVEEIKKENI PASISNTAGT FVCNHLMYGI LNYVHKNGLN IKAGFIHIPY LPVQVLNKPY
TPSMSLGDMV KAIETAIKVI AKKSR
//
