ID D1NVJ8_9BIFI Unreviewed; 229 AA.
AC D1NVJ8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=BIFGAL_03887 {ECO:0000313|EMBL:EFA22849.1};
OS Bifidobacterium gallicum DSM 20093 = LMG 11596.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA22849.1, ECO:0000313|Proteomes:UP000003656};
RN [1] {ECO:0000313|EMBL:EFA22849.1, ECO:0000313|Proteomes:UP000003656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA22849.1,
RC ECO:0000313|Proteomes:UP000003656};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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:EFA22849.1}.
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DR EMBL; ABXB03000003; EFA22849.1; -; Genomic_DNA.
DR AlphaFoldDB; D1NVJ8; -.
DR STRING; 561180.BIFGAL_03887; -.
DR eggNOG; COG2039; Bacteria.
DR Proteomes; UP000003656; Unassembled WGS sequence.
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 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 229 AA; 25008 MW; 7CF5F740D41F572E CRC64;
MMNTAANSEP TRLSVLISGF GPYDHVPVNP SQLVPKLLAE QGIAANPGDL DDPLRGVQLD
VHAVTMPVSY AGSWAMLERE LERVQPDIVV ATGLKRAARG ILLERGALNR TDSTRPDADD
VVADRGPIRE GAPAAYWTRL PLRAILNAFS KDHTLPASLT SDAGTFVCNA LFYQLQDWAA
HQTRDVLTGF VSLPLINDEP HPQHGLPLER QVVAIRHVVR QSVAYLLDM
//
