ID E8PRB6_THESS Unreviewed; 193 AA.
AC E8PRB6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
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 Name=pcp {ECO:0000313|EMBL:ADW21945.1};
GN OrderedLocusNames=TSC_c13250 {ECO:0000313|EMBL:ADW21945.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21945.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW21945.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR EMBL; CP001962; ADW21945.1; -; Genomic_DNA.
DR RefSeq; WP_015717218.1; NC_014974.1.
DR AlphaFoldDB; E8PRB6; -.
DR STRING; 743525.TSC_c13250; -.
DR MEROPS; C15.001; -.
DR KEGG; tsc:TSC_c13250; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_3_0; -.
DR Proteomes; UP000008087; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
SQ SEQUENCE 193 AA; 21047 MW; 0F1F238A0C31E75B CRC64;
MILVTGFEPF GGLKHNPSAT LLERLPQGVG DHPLHKAILP VDSAALPGVL RKLHALKPKV
VLHLGLAEGR PLLSLERLAI NLLDFERPDN RGIRWEDTPV VPGGPLALEA RFPLKESLRR
LREAGIPAKQ SLSAGSYLCN QAFYLSLFHL PPEVPVGFVH LPPDETLALE RGGAYLPLAE
QVRAVTLLLD TLL
//
