ID   A0A3B7MW10_9BACT        Unreviewed;       770 AA.
AC   A0A3B7MW10;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=S9 family peptidase {ECO:0000313|EMBL:AXY78674.1};
GN   ORFNames=D3H65_16790 {ECO:0000313|EMBL:AXY78674.1};
OS   Paraflavitalea soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Paraflavitalea.
OX   NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY78674.1, ECO:0000313|Proteomes:UP000263900};
RN   [1] {ECO:0000313|EMBL:AXY78674.1, ECO:0000313|Proteomes:UP000263900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY78674.1,
RC   ECO:0000313|Proteomes:UP000263900};
RA   Weon H.-Y., Heo J., Kwon S.-W.;
RT   "Genome sequencing of strain 6GH32-13.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP032157; AXY78674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7MW10; -.
DR   KEGG; pseg:D3H65_16790; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000263900; Chromosome.
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:SF118; BLR1971 PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..770
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017682195"
FT   DOMAIN          177..465
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          551..728
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   770 AA;  86236 MW;  B4905EB445F357E9 CRC64;
     MHKIVPVILM AVTLFNRPLT AQTVTRFQPS HEAMVQRYLR AARIDSATKN AVFKSTVTIS
     WLPGGKTAWY QNLLKDSVQE YIYVDAVKGK KQPLFHRQRL AEGLQQIGIT IDSLRPSLSN
     IDIPVGKPFL YFTVQGQRVQ CERNSHVCAK TPMLAPPAGN TPGAFRGRQN NPFPNGSTSP
     DKQWEAYIEK GNLVVKPAAG GTPIQFTTDG TPEKPYGTIY WSPDSKYLAG YHINTVRDSS
     VYYILTSLPG TMRGQLRSQS YKQPGDPWTI YTPWLFQLSS KKAVKINTGP VDFLNAPALT
     WRSGNARYFT YEKMDRGHQR FRVIEVDADN ATTRNVVDEK TSTFIYNTRN FTSYLSPTNQ
     LIRTSEKEGW NHIYLVDLVT GKEQPVTRGN WVIRGVDSID PVKKEVWFRA SGMQAGEDPY
     NIHYYRIGFD GKNLKSLTPA AGNHTLAFSD DKTYFIDTWS QVNIAPRTIL ARTADAKEIM
     LLEEADLSLY KRAGVSPPEV FVAKARDGVT DIWGIVSKPS DYDPSKKYPV LENIYAGPHD
     AFVPKNFVPY SEMQSLAELG FIVVMIDGMG TANRSKAFHD VCWKNLADAG LPDRILWIKA
     LAQKYPYVDA ERVGIYGTSA GGQSSTGALL FHPEFYKAAV SACGCHDNRV DKQWWNEQWM
     GYPVGKHYEE QSNVTNAAKL QGNLLLIVGE ADTNVPPEST YRVADALIKA GKNFDLLSIP
     GMGHSDGGVY GRMRKRDFFV KHLMGVEPPA RNAGELPAFA EVGRERWSFQ
//