ID U7L6I2_9CORY Unreviewed; 157 AA.
AC U7L6I2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10076};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10076};
GN ORFNames=HMPREF1264_02097 {ECO:0000313|EMBL:ERS53536.1};
OS Corynebacterium sp. KPL1821.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203560 {ECO:0000313|EMBL:ERS53536.1, ECO:0000313|Proteomes:UP000017152};
RN [1] {ECO:0000313|EMBL:ERS53536.1, ECO:0000313|Proteomes:UP000017152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1821 {ECO:0000313|EMBL:ERS53536.1,
RC ECO:0000313|Proteomes:UP000017152};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1821.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000256|ARBA:ARBA00002280}.
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|ARBA:ARBA00001770,
CC ECO:0000256|PROSITE-ProRule:PRU10076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERS53536.1}.
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DR EMBL; AXLZ01000013; ERS53536.1; -; Genomic_DNA.
DR AlphaFoldDB; U7L6I2; -.
DR PATRIC; fig|1203560.3.peg.2023; -.
DR HOGENOM; CLU_043960_4_0_11; -.
DR Proteomes; UP000017152; Unassembled WGS sequence.
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 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 InterPro; IPR033693; PGPEP1_Glu_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; PS01333; PYRASE_GLU; 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:UP000017152};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10076"
SQ SEQUENCE 157 AA; 16864 MW; 277C921F3851BB40 CRC64;
MIPTKFGESL RRVIALAEES SVDAIVCLGQ AGGRKHITPE RVAINVMDAE IPDNAGYQPV
DVPVVEGGPA AYFSTLPVKE MVAAMDDCPA RVSNTAGTFV CNQLLYGLLH HFAGTEVRAG
FVHVPYIEEQ NKADKPMMAL AEVVEGIKRA LWAVQAS
//
