ID A0A1M7QRH8_9SPHI Unreviewed; 704 AA.
AC A0A1M7QRH8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05216524_1118 {ECO:0000313|EMBL:SHN34244.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHN34244.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHN34244.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHN34244.1,
RC ECO:0000313|Proteomes:UP000184158};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCM01000011; SHN34244.1; -; Genomic_DNA.
DR RefSeq; WP_073407319.1; NZ_FRCM01000011.1.
DR AlphaFoldDB; A0A1M7QRH8; -.
DR STRING; 1855297.SAMN05216524_1118; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000184158; 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..704
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009928880"
FT DOMAIN 30..430
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 488..701
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 704 AA; 78047 MW; DF98E1CF25B87531 CRC64;
MKTITCLSAA VLICSFALAQ QMNPKTIAYP ATKKVDTVNN YFGTEVPDPY RWLEDDRAAD
TKAWVQAENK VTQDYLGQIP YRDAMHARLK QLWNYEKYSA PFKEGKYTYF YKNDGLQSQS
VLWRQVGDGA PEIFLDPNKF SADGTTSLQG IDFTKDGSMA AYQLSEGGSD WRKVIVIKTA
DNSMVGDTLI DIKFSGIAWK GNEGFYYSSY DKPKAGSQLA GITQYHKLFY HKLGTAQSSD
VLIFGGDKTP RRYIGAGLTE DEHFLVISAA KETTGNELYI QDLSSPNSLI INVVDNFDNQ
HSVLGNVGSK LYIITNLYEP NFKIVTVDAA DPKTKNWKDL VPATGNVLSA TTGGGKIFAE
YLKDATSFVQ QYNMDGKLER TITLASIGTA SGFGAKLKEK ETYYTFTNYV YPGTIFKLDI
ATGTSTVYKK SGVQFNPEQY ESKQVFYKSK DGTKIPMLIT YKKGTVMNGK NPLLLYAYGG
FGVNLTPAFS TSNIILVEHG GIYAVPNLRG GGEYGEKWHK AGIKMKKQNV FDDFIAAAEY
LIKNKYTSKD YLAISGGSNG GLLIGAVMTQ RPDLCKVALP AVGVMDMLRY NQFTAGAGWS
YDYGTAQDNK EMFAYLYKYS PYHALKPASY PATMVTTADH DDRVVPAHSF KFAARLQEYQ
KGPAPTLIRI ETKAGHGAGQ STEQVISGQV DKWAFMFWNM GVKF
//
