(data stored in SCRATCH zone)

SWISSPROT: B2UHL3_RALPJ

ID   B2UHL3_RALPJ            Unreviewed;       215 AA.
AC   B2UHL3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=Rpic_3959 {ECO:0000313|EMBL:ACD29064.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29064.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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       ECO:0000256|SAAS:SAAS01095886}.
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         ECO:0000256|SAAS:SAAS01127808};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00417,
CC       ECO:0000256|SAAS:SAAS01095894}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00417, ECO:0000256|SAAS:SAAS01084667}.
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DR   EMBL; CP001069; ACD29064.1; -; Genomic_DNA.
DR   RefSeq; WP_012430089.1; NC_010678.1.
DR   STRING; 402626.Rpic_3959; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; ACD29064; ACD29064; Rpic_3959.
DR   GeneID; 6285196; -.
DR   KEGG; rpi:Rpic_3959; -.
DR   PATRIC; fig|402626.5.peg.198; -.
DR   eggNOG; ENOG4108KN7; Bacteria.
DR   eggNOG; COG2039; LUCA.
DR   HOGENOM; HOG000242641; -.
DR   KO; K01304; -.
DR   OMA; HHIATRA; -.
DR   OrthoDB; 1927224at2; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00501; Peptidase_C15; 1.
DR   Gene3D; 3.40.630.20; -; 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   PANTHER; PTHR23402; PTHR23402; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; SSF53182; 1.
DR   TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR   PROSITE; PS01334; PYRASE_CYS; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UHL3.
DR   SWISS-2DPAGE; B2UHL3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS01095881};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS01084660, ECO:0000313|EMBL:ACD29064.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS01084657};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Thiol protease {ECO:0000256|HAMAP-Rule:MF_00417,
KW   ECO:0000256|SAAS:SAAS01084664}.
FT   ACT_SITE     80     80       {ECO:0000256|HAMAP-Rule:MF_00417}.
FT   ACT_SITE    143    143       {ECO:0000256|HAMAP-Rule:MF_00417,
FT                                ECO:0000256|PROSITE-ProRule:PRU10077}.
FT   ACT_SITE    167    167       {ECO:0000256|HAMAP-Rule:MF_00417}.
SQ   SEQUENCE   215 AA;  22635 MW;  ED36C6CE5C066754 CRC64;
     MTTVLVTGIE PFESDPTNPS WDIAQALDST QVDSAVIVAR QLPCVFGLAN EILVDAIEAT
     SPALVFALGL ATGRTEISVE RVAINVIDAR IPDNAGNQPV DTPVVADGPT AYFSTLPIKA
     IVHALREAGV PAGVSQSAGT YNCNHLFYGL MHHIAMRAPQ VRGGFIHVPT TPELAARHAG
     RPSLSIDTQI KGIRLAVRTT LATQSDLKMS AGAVH
//

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