ID F0NUD0_LACHH Unreviewed; 200 AA.
AC F0NUD0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 74.
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=LBHH_0191 {ECO:0000313|EMBL:ADX69427.1};
OS Lactobacillus helveticus (strain H10).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=767462 {ECO:0000313|EMBL:ADX69427.1, ECO:0000313|Proteomes:UP000008640};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H10;
RA Zhang H., Zhao W., Chen Y., Sun Z., Sun T., Meng H.;
RT "Complete genome sequence of Lactobacillus helveticus strain H10.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADX69427.1, ECO:0000313|Proteomes:UP000008640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H10 {ECO:0000313|EMBL:ADX69427.1,
RC ECO:0000313|Proteomes:UP000008640};
RX PubMed=21398542; DOI=10.1128/JB.00166-11;
RA Zhao W., Chen Y., Sun Z., Wang J., Zhou Z., Sun T., Wang L., Chen W.,
RA Zhang H.;
RT "Complete genome sequence of Lactobacillus helveticus H10.";
RL J. Bacteriol. 193:2666-2667(2011).
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; CP002429; ADX69427.1; -; Genomic_DNA.
DR RefSeq; WP_014562919.1; NC_017467.1.
DR AlphaFoldDB; F0NUD0; -.
DR MEROPS; C15.001; -.
DR KEGG; lhl:LBHH_0191; -.
DR PATRIC; fig|767462.3.peg.214; -.
DR HOGENOM; CLU_043960_4_0_9; -.
DR Proteomes; UP000008640; 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 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 200 AA; 21686 MW; 9DD4886AB2F2B0B7 CRC64;
MKILVTGFDP FGGEKINPAI EAVKRLPDEI AGNQIIKLEV PTIFYQSAEV VKKAIEKENP
EMVINVGQAG GRSAITPERI AINFQAGSTP DNSGKGPKEG KIQADGLDGY FTQLPIKKMV
TAIRHAGLPA QVSNSAGTYV CNHLFYEIQY LIHHDYPNLK AGFIHIPYLP SQAKNGRYPS
MSLDNMVTGL TAAIETAAMC
//
