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Database: UniProt
Entry: F4KNQ6_PORAD
LinkDB: F4KNQ6_PORAD
Original site: F4KNQ6_PORAD 
ID   F4KNQ6_PORAD            Unreviewed;       201 AA.
AC   F4KNQ6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000256|ARBA:ARBA00019191};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000256|ARBA:ARBA00030836};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000256|ARBA:ARBA00031559};
GN   OrderedLocusNames=Poras_1572 {ECO:0000313|EMBL:AEE13503.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS   JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE13503.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family.
CC       {ECO:0000256|ARBA:ARBA00006641}.
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DR   EMBL; CP002689; AEE13503.1; -; Genomic_DNA.
DR   RefSeq; WP_013760836.1; NC_015501.1.
DR   AlphaFoldDB; F4KNQ6; -.
DR   STRING; 879243.Poras_1572; -.
DR   MEROPS; C15.001; -.
DR   KEGG; pah:Poras_1572; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_0_10; -.
DR   OMA; HHIATRA; -.
DR   Proteomes; UP000006545; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:InterPro.
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   InterPro; IPR000816; Peptidase_C15.
DR   InterPro; IPR016125; Peptidase_C15-like.
DR   InterPro; IPR036440; Peptidase_C15-like_sf.
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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEE13503.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
SQ   SEQUENCE   201 AA;  22433 MW;  21936DFA407AA07D CRC64;
     MTGFEPYWNY PENSSWVVAQ EVATHDLAGV RIYTELMPVS FHQVAAALRR AIDQHTPDLI
     IMLGQSGGSD RVKLERIAIN MMDSKLPDNE GYLPDEEIIY ANGSSALFTN TAIKELRTTI
     EQLGIKVKIS NSSGLYVCNR LYYEALSVAQ SRPSTQVLFV HLPYYEGQPS AKPEKPTMPL
     DDMVRAIVAI IERTCGTHQA I
//
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