ID   A0A238X9D2_9FLAO        Unreviewed;       845 AA.
AC   A0A238X9D2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Prolyl oligopeptidase family protein {ECO:0000313|EMBL:SNR55123.1};
GN   ORFNames=SAMN04488111_1678 {ECO:0000313|EMBL:SNR55123.1};
OS   Lutibacter flavus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=691689 {ECO:0000313|EMBL:SNR55123.1, ECO:0000313|Proteomes:UP000198412};
RN   [1] {ECO:0000313|Proteomes:UP000198412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27993 {ECO:0000313|Proteomes:UP000198412};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; FZNX01000002; SNR55123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238X9D2; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000198412; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..845
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012444124"
FT   DOMAIN          196..535
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          624..810
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          134..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  97725 MW;  A4331174C5F9F7C1 CRC64;
     MKKIIVLLFV MGTCVVFAQN YEATKVPTPN YRLASKFSPT NLAKLVHSTN VRPNWLKKGN
     RFWYQYKTTN GSNYYLVDAD RRTKTKLFDN DKMAEWLTEI TKDPYDGQHL PKFDFKFVKD
     ETAIQFRVTS TEEVEAKDEK KDEDTEDEEK EDVKKDSTDT KKAKKKKPKM EKKVYHLEYR
     LGGRGLTVIG NSKKEDKLKR WANIAPDSSI VLFSKNYNLY WMDKENFLKA IKDDKDTTIV
     ENQWTKDGVE HYGYGGSGRG ENNETKEEKK DDRKGVRGIW TRDSKKFIYE RSDSRHIKDL
     WVINSVSKKR PTLETYKYHM PGEQEYYKFE LQVFDIPSKN VMNVKLDTSK QQSINVYRHR
     YKKSEASDEF KPSLLLSKKG KIYFSTISRD RKKLDICVAD ILTGDVEVLI EERFNTYIEE
     QQLVLFNNET EMLYWAERDG WAHYYLYDSK GNLKNQITNG AYHVDGFNGI DEKERVLYFT
     ANGVNKSIDP YYAHLYRINL DGSGLRNINS GDFTTNVSTS DSNKYFVSNF SRVDSTPKSE
     LRSNTGALIM SLEEADLTQL FATGYKFPET FKMKANDGIT DIYGVMYKPF DFDATKSYPL
     LEYVYPGPQT EAVNKAFSVR MDRLDRMAQV GFIVVTMGNR GGHPDRSKWY HNYGYGNLRD
     YGLADKKYVA EQLADSFDFI DINKVGIYGH SGGGFMSTAA MLVYPDFFKA AVSSAGNHDN
     SMYNSWWSET HHGVKEEIEA DGSIEHKYDI DKNQSLAANL KGNLMLIHGD IDNNVHPGGT
     IRMADALIKA NKRFKFMVMP GQRHGFGKMT EYSFWLRADH FSKYFLGEEA TSVDILEMNR
     DKPKK
//