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Database: UniProt
Entry: A0A1H4S4X3_9FLAO
LinkDB: A0A1H4S4X3_9FLAO
Original site: A0A1H4S4X3_9FLAO 
ID   A0A1H4S4X3_9FLAO        Unreviewed;       721 AA.
AC   A0A1H4S4X3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN04489761_2862 {ECO:0000313|EMBL:SEC39088.1};
OS   Tenacibaculum sp. MAR_2009_124.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEC39088.1, ECO:0000313|Proteomes:UP000199366};
RN   [1] {ECO:0000313|EMBL:SEC39088.1, ECO:0000313|Proteomes:UP000199366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEC39088.1,
RC   ECO:0000313|Proteomes:UP000199366};
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; FNSF01000005; SEC39088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4S4X3; -.
DR   STRING; 1250059.SAMN04489761_2862; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000199366; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199366}.
FT   DOMAIN          35..433
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          493..706
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   721 AA;  80557 MW;  A25ED3182B03FE4C CRC64;
     MKKIIFPVLA ASFILVSCEK PVNKITKRDI AVTYPATDKK PIVDDYFGTK VTDNYRWLED
     DRSTETENWV KAENEVTFDY LSKIPYRTQL KDRLSELWNF EKVGTPFEEG EYTYYFKNDG
     LQNQYVLYRT DKNGKDEVFL DPNTFAEDGT TSLGNLSFTK DGKTLAYSIS EGGSDWQKVI
     IMDAETREIK GDTLVDVKFS GISWKGNEGF YYSSYDKPKG SALSAKTDQH KLYFHLLGTP
     QSADQVIFGA TPEEKHRYVG GSLTEDDRYL LVSASTSTSG NKLFIKDLSN PKSKLTPIIN
     NFDSDTYLIE NKGTKLYLVT NLNAPNKKIV TVDANNPTPE NWKDFIPETE NVLSPSTGGG
     FFFTKYMVDA VSKVLQYDYE GKLIREIKLP GVGTAGGFGG KKEEKELYFS FTNYNTPGSS
     YKYNVEEGSY ELYWKPSISF NSDDYESKQV FFTSKDGTKV PMIITHKKGL ELNGKNPTIL
     YGYGGFNVSL TPGFSIANAV WMEQGGVYAV PNLRGGGEYG KKWHNAGIQM KKQNVFDDFI
     AAGEYLIESK YTSSDFLAIR GGSNGGLLVG ATMTQRPDLM KVALPAVGVL DMLRYHTFTA
     GAGWAYDYGT SEQSKEMFDY LKGYSPVHNV KSEIEYPATL VTTGDHDDRV VPAHSFKFAA
     ELQDKQNGNN PVLIRIETNA GHGAGTPVAK TIEQYADIFG FTLFNMGFDS LPNPPKSKIK
     S
//
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