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Database: UniProt
Entry: G3A8G7_9RALS
LinkDB: G3A8G7_9RALS
Original site: G3A8G7_9RALS 
ID   G3A8G7_9RALS            Unreviewed;       215 AA.
AC   G3A8G7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   13-SEP-2023, entry version 45.
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   ECO:0000313|EMBL:CCA87541.1};
GN   ORFNames=RALSY_mp10056 {ECO:0000313|EMBL:CCA87541.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA87541.1};
RN   [1] {ECO:0000313|EMBL:CCA87541.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA87541.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA87541.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA87541.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {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|HAMAP-Rule:MF_00417,
CC         ECO:0000256|PROSITE-ProRule:PRU10077};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; FR854090; CCA87541.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3A8G7; -.
DR   MEROPS; C15.001; -.
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   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.
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   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   215 AA;  22550 MW;  F0EEAD4B4A85A9CC CRC64;
     MTTVLITGIE PFESDPINPS WEIARALDGE RIDGATLVAR QLPCVFGRAN LELVAAIEAT
     QPSLVLALGL ASGRSEISVE RVAINVIDAR IPDNAGHQPV DVPVVADGPA AYFSSLPIKA
     IVHALRAAGV PAAVSQSAGT YNCNHLFDGL MHHIATRAPR MRGGFIHVPT TPELAARHPG
     RPSLPLDTQT AGMRVAVRTA LATQSDLTLS GGTLH
//
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