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Database: UniProt
Entry: R0M7P7_STRMT
LinkDB: R0M7P7_STRMT
Original site: R0M7P7_STRMT 
ID   R0M7P7_STRMT            Unreviewed;       214 AA.
AC   R0M7P7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=D065_09777 {ECO:0000313|EMBL:EOB31006.1};
OS   Streptococcus mitis 13/39.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1239793 {ECO:0000313|EMBL:EOB31006.1, ECO:0000313|Proteomes:UP000013315};
RN   [1] {ECO:0000313|EMBL:EOB31006.1, ECO:0000313|Proteomes:UP000013315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13/39 {ECO:0000313|EMBL:EOB31006.1,
RC   ECO:0000313|Proteomes:UP000013315};
RA   Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Semashko T.A.,
RA   Karpova I.Y.U., Larin A.K., Ischenko D.S., Alekseev D.G., Klimova E.A.,
RA   Filimonova A.V., Savinova T.A., Filimonova O.Y.U., Dubovickaya V.A.,
RA   Sidorenko S.V., Govorun V.M.;
RL   Submitted (APR-2013) 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:EOB31006.1}.
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DR   EMBL; AQTU01000040; EOB31006.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0M7P7; -.
DR   PATRIC; fig|1239793.3.peg.1905; -.
DR   Proteomes; UP000013315; 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;  23383 MW;  701AC971174983F2 CRC64;
     MKVLVTGFEP FGGEKVNPAL EAIKGLPAEI HGAEVRWLEV PTVFHKSAHV LEEEMNRYQP
     DFVLCIGQAG GRSSLTPERV AINQDDARIP DNEGNQPIDL PIRSDGAPAY FSSLPIKAMV
     QAIKKEGLPA SVSNTAGTFV CNHLMYQALY LVEKKFPHVK AGFMHIPYMM EQVVNRPTTP
     AMSLVDIMRG VEAAIGAIIE HGDQDLKLVG GETH
//
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