ID D8JT47_HYPDA Unreviewed; 186 AA.
AC D8JT47;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10077};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10077};
GN OrderedLocusNames=Hden_2569 {ECO:0000313|EMBL:ADJ24365.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ24365.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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|PROSITE-ProRule:PRU10077};
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR EMBL; CP002083; ADJ24365.1; -; Genomic_DNA.
DR AlphaFoldDB; D8JT47; -.
DR STRING; 582899.Hden_2569; -.
DR KEGG; hdn:Hden_2569; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_1_5; -.
DR Proteomes; UP000002033; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR033694; PGPEP1_Cys_AS.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF1; RE07960P; 1.
DR Pfam; PF01470; Peptidase_C15; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
SQ SEQUENCE 186 AA; 19976 MW; 414F935D1AC77BB5 CRC64;
MIVKRLAREA RLALPHVRFA VAVLPTDWAR APGLISELHE RHDPVLALHF GVATSMRGFR
IETEARNFCR MSPDAAGGLP ASNCICEGGA SALSTSIPAT AVAQHLEAQG FEARLSDDAG
GYLCNAVFYH SLLEASTRRD RCRVGFIHIP VEAGEPEAVD RTVAGALEVL KFSLHHAPQV
ATLTSV
//
