ID A0A1I0PLH9_9BACT Unreviewed; 702 AA.
AC A0A1I0PLH9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=SAMN04487827_1854 {ECO:0000313|EMBL:SEW15199.1};
OS Prevotella sp. khp7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761885 {ECO:0000313|EMBL:SEW15199.1, ECO:0000313|Proteomes:UP000198798};
RN [1] {ECO:0000313|EMBL:SEW15199.1, ECO:0000313|Proteomes:UP000198798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHP7 {ECO:0000313|EMBL:SEW15199.1,
RC ECO:0000313|Proteomes:UP000198798};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOIV01000003; SEW15199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0PLH9; -.
DR STRING; 1761885.SAMN04487827_1854; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000198798; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..702
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011463673"
FT DOMAIN 26..426
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 483..698
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 702 AA; 80180 MW; 52D54E0A5A6E4DC6 CRC64;
MKKIGIISMA IMVTTMVQAQ SSMQYPQTEK DNTVDEYFGV KVSDPYRWLE NDTSAQTTAW
VEAENKVTST YLRKIPFRDK LLKRLTELSN YEKIGAPSKH HNKWYFSRNN GLQNQSVIYV
MDKLDGKPRI FLDPNTLSAD GTVALKSISF SNNGRWAAYA ISRSGSDWQE FYVIDVNTGQ
LTNDHIEWAK FSDATWLGDG FYYSAYDRPI EYKEFSNLNS GHKIYYHKIG TSQSDDVLFY
QNPTEPMRFY NVEINEDETV MYLYESGAGA GNILYVRDLR QKDAQFVKMT SDMNYQYSPI
YSNDDKLYIY TNYGAPKGRI MMVDIHKPGI NDWQELIPEQ QNVLGSATVI NRQLVLTYSQ
DASDHAFIYG LDGQMRHEVK LPMVGSVNFS GNEKESDCFY TFTSFTQPGT VYRYDIDANL
STIYAQPRVK FRLQDYESRQ LFFESKDGTR IPMYITYKKG MKRSGKNPVY LYGYGGFNIA
LTPSFSSTRI PFLEQGGIYA QVNLRGGSEY GEEWHLAGTK MQKQNVFDDF IAAAEYLIKE
KYTCSDRLAI VGGSNGGLLV GACMTQRPDL YHVAIPQVGV MDMLRYHKFT IGWNWASDYG
TSDDSKEMFE YLRTYSPLHN LKPGISYPAT LVTTADHDDR VVPAHSFKFT ATLQECHKGL
NPVLIRIDTK AGHGGGKPLA KVLEEQADIY SFILFNMGMK FK
//
