ID A0A370IBM1_9NOCA Unreviewed; 675 AA.
AC A0A370IBM1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=DFR76_102411 {ECO:0000313|EMBL:RDI68010.1};
OS Nocardia pseudobrasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=45979 {ECO:0000313|EMBL:RDI68010.1, ECO:0000313|Proteomes:UP000254869};
RN [1] {ECO:0000313|EMBL:RDI68010.1, ECO:0000313|Proteomes:UP000254869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44290 {ECO:0000313|EMBL:RDI68010.1,
RC ECO:0000313|Proteomes:UP000254869};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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:RDI68010.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQBC01000002; RDI68010.1; -; Genomic_DNA.
DR RefSeq; WP_067992433.1; NZ_QQBC01000002.1.
DR AlphaFoldDB; A0A370IBM1; -.
DR STRING; 1210086.GCA_001613105_00987; -.
DR Proteomes; UP000254869; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000254869}.
FT DOMAIN 10..400
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 466..669
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 675 AA; 72853 MW; 96465910F0B0F079 CRC64;
MTAEYPCAPA EETWDDLHGM RIRDPFRPLE DPADPRNLAW VAAQRELTET YLAELPGQQR
LQELLRDIII QGPTASPVKS AGKRRFRVGR ARVASPWQLQ VADGPEDRWR TLLDAAALGP
GAILRRWTPS PDGRFVAVQA SVGGSETSTP LALIDAETGA VLRTCALTRY APVEWLADGS
GYYYVRRHEN RCGSGVYLHR IDTEIADDEL LVGDEDPVGR YHLTFWHDRW LILTGRSGTS
RNTRVSIVDV AEGGSPRPLD LGGLSSAGVV VDRDGRILAL STAESEFGQL LVSEPDVSEG
AWRVLVPADE PAVLAAFAVA PAEDGDRLLI LRTRDGYAEL SIHDARSGAW LFDAELPGAG
TVAAIKSTDE PGVLVLSYTD WIRPLGAWRL DLRTGRITPT EPAARVLPGI TVIRTTYRSA
DDTEVPLTVL APRGPRIPRP AILSCYGGFG ITFRPGYQPD GLTWVLAGGV MAIAGVRGGG
ERGRRWHLDG AGVRKLNAFA DLHAAGDWLV DTGWTRRGQL ALLGGSNGGL MAVGAMVQRP
SAYAAVVSAG APLDMVRYER WGLGRAWREE YGSAADPTAL AVLLRYSPYH NVTAHLDEPP
RHWPPALFTT GDSDTRVPPV HSCKMVAALQ REIGGPILLD VIAGKGHAGG GPASDRALIL
LLAFVARHTG LPLLD
//