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Database: UniProt
Entry: J6YWK2_ENTFC
LinkDB: J6YWK2_ENTFC
Original site: J6YWK2_ENTFC 
ID   J6YWK2_ENTFC            Unreviewed;       214 AA.
AC   J6YWK2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 67.
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   ORFNames=HMPREF1348_01703 {ECO:0000313|EMBL:EJY45024.1};
OS   Enterococcus faecium 505.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1134806 {ECO:0000313|EMBL:EJY45024.1, ECO:0000313|Proteomes:UP000006403};
RN   [1] {ECO:0000313|EMBL:EJY45024.1, ECO:0000313|Proteomes:UP000006403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=505 {ECO:0000313|EMBL:EJY45024.1,
RC   ECO:0000313|Proteomes:UP000006403};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJY45024.1}.
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DR   EMBL; AMBL01000054; EJY45024.1; -; Genomic_DNA.
DR   RefSeq; WP_002287081.1; NZ_JH813169.1.
DR   AlphaFoldDB; J6YWK2; -.
DR   GeneID; 66496852; -.
DR   PATRIC; fig|1134806.3.peg.1622; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   Proteomes; UP000006403; Unassembled WGS sequence.
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        78
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT                   ECO:0000256|PROSITE-ProRule:PRU10076"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417,
FT                   ECO:0000256|PROSITE-ProRule:PRU10077"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00417"
SQ   SEQUENCE   214 AA;  23094 MW;  9FF39263FD33DF28 CRC64;
     MKVLVTGFDP FGGDKVNPAY EAVKKMPDEI SGAEIIKVEV PTVFEKSSQV VKEAIQQHQP
     DVVICVGQAG GRSAVSFERV AINLAEARIP DNEGNQPFDT ALEENGPAAY FTSLPIKAMT
     KNVQDHGLPA YISYTAGTFV CNDIMYRLLH LIETQFPAIR GGFIHVPFSP DQVIDRPVGT
     PSMSLEDIAS SLTYAVEAAV ENKEDISGNA GTTH
//
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