(data stored in ACNUC7421 zone)

SWISSPROT: PCP_SULIK

ID   PCP_SULIK               Reviewed;         209 AA.
AC   C4KEG7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN   Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417};
GN   OrderedLocusNames=M164_0533;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal pyroglutamyl group
CC       from a polypeptide, the second amino acid generally not being Pro.
CC       {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00417}.
DR   EMBL; CP001402; ACR41164.1; -; Genomic_DNA.
DR   RefSeq; WP_010923507.1; NC_012726.1.
DR   ProteinModelPortal; C4KEG7; -.
DR   SMR; C4KEG7; -.
DR   EnsemblBacteria; ACR41164; ACR41164; M164_0533.
DR   GeneID; 8760370; -.
DR   KEGG; sid:M164_0533; -.
DR   HOGENOM; HOG000242641; -.
DR   KO; K01304; -.
DR   OMA; HHIATRA; -.
DR   OrthoDB; POG093Z0BJN; -.
DR   BioCyc; SISL426118:GI01-545-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
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:InterPro.
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; IPR029762; PGP-I_bact-type.
DR   InterPro; IPR033694; PGPEP1_Cys_AS.
DR   InterPro; IPR033693; PGPEP1_Glu_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   PROSITE; PS01334; PYRASE_CYS; 1.
DR   PROSITE; PS01333; PYRASE_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KEG7.
DR   SWISS-2DPAGE; C4KEG7.
KW   Complete proteome; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN         1    209       Pyrrolidone-carboxylate peptidase.
FT                                /FTId=PRO_1000206025.
FT   ACT_SITE     79     79       {ECO:0000255|HAMAP-Rule:MF_00417}.
FT   ACT_SITE    142    142       {ECO:0000255|HAMAP-Rule:MF_00417}.
FT   ACT_SITE    164    164       {ECO:0000255|HAMAP-Rule:MF_00417}.
SQ   SEQUENCE   209 AA;  23404 MW;  AAE205344FD024B7 CRC64;
     MTVLLFGFEP FLEYKENPSQ LIVEALNGST ILKEEVKGVI LPVEYEKIED LIVTKIREMK
     PILTLGIGVA PGRAKITPEK IAINYKYSRE GDNAGKKYKG EKIDPLGQDG IFTNIPVEDL
     VDLLNENGIP AELSLSAGSY LCNNAMYIII REARKYNSLG GFIHVPLHES YAARIQRPIP
     SMSLDTMIRG IRLSMEFILT NKKENLTFS
//

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