ID   A0A1M3G4G7_9SPHI        Unreviewed;       777 AA.
AC   A0A1M3G4G7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=S9 family peptidase {ECO:0000313|EMBL:OJW34927.1};
GN   ORFNames=BGO54_06465 {ECO:0000313|EMBL:OJW34927.1};
OS   Sphingobacteriales bacterium 46-32.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW34927.1, ECO:0000313|Proteomes:UP000184358};
RN   [1] {ECO:0000313|EMBL:OJW34927.1, ECO:0000313|Proteomes:UP000184358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46-32 {ECO:0000313|EMBL:OJW34927.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJW34927.1}.
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DR   EMBL; MKTY01000015; OJW34927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3G4G7; -.
DR   STRING; 1895839.BGO54_06465; -.
DR   Proteomes; UP000184358; 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: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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..777
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012251161"
FT   DOMAIN          118..476
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          566..758
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          144..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  86943 MW;  29BB468B9F5789DA CRC64;
     MSKHLIALAA LSATLTATAQ RTDSLSRKDY EHAASFLGFG TESLVYRTNL RANWMDGDKF
     WYGINTEKGT EFFLVDPAKK SKAPAFDQNK LAAALSTSLG RNVDPYKLPF QQFTYASDMQ
     SVSFSADSKR WKYVLKSGVL TQETGTAPAE TAPAQPMGRR GGGSDVVSPD GKKAAFIKDY
     NLWVRDVATK KETQLTTDGI KDFGYATDNA GWSSSDRPIL RWSPDSKKIA TFQQDQRKVG
     DMYLVTTNVG HPTLRAWKYP LPGDKDIAMI HRVIINVDEP KVIRLQVAPD PHRASLSDDI
     SSSGTFDDVD WKADGTELAF LSTSRDHKIE KMRIADASTG AVREVFEERV ATQYESGQGA
     INWRYLAATN EFIWYSERDD WGHLYLYDAK TGQLKNQITK GSFVVTRMLE VDEKKREITF
     IGLGNDPVNP YFGRVYRVSF DGKKMTDLTP ATGNHMAVFS PSKKYLIDTY SQPDVPSTMV
     LRDAATGKQL VELEKTDVSK LQEAKGWKAP AVVKVKAHDN KTDIYGLVFT PTKMEAGKKY
     PVVDYIYPGP QGGSVGSWSF SASRGDHQAL AELGFIVVLI EGTSNPDRSK SFHDMSYGNM
     AENTLPDQIA AIRQLSQTYP MDTTKVGIWG HSGGGFATAA AMFRYPDFFK VGISESGNHD
     NRNYEDDWGE RYNGLVENSN YEAQANQNYA QNLKGKLMLA HGMMDNNVPP YNTLLVVEAL
     EKANKDYDLV IFPNSAHGFG QYSYYMMRRR WDYFVKNLRG IEPPKEFELK APAPTRR
//