ID   A0A1D7QGB1_9SPHI        Unreviewed;       706 AA.
AC   A0A1D7QGB1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptidase S9 {ECO:0000313|EMBL:AOM77700.1};
GN   ORFNames=BFS30_11275 {ECO:0000313|EMBL:AOM77700.1};
OS   Pedobacter steynii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM77700.1, ECO:0000313|Proteomes:UP000094313};
RN   [1] {ECO:0000313|EMBL:AOM77700.1, ECO:0000313|Proteomes:UP000094313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX4 {ECO:0000313|EMBL:AOM77700.1,
RC   ECO:0000313|Proteomes:UP000094313};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017141; AOM77700.1; -; Genomic_DNA.
DR   RefSeq; WP_069379388.1; NZ_CP017141.1.
DR   AlphaFoldDB; A0A1D7QGB1; -.
DR   KEGG; psty:BFS30_11275; -.
DR   OrthoDB; 9777457at2; -.
DR   Proteomes; UP000094313; Chromosome.
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; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094313};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..706
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009098537"
FT   DOMAIN          100..416
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          501..696
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   706 AA;  80669 MW;  8BE7B0165A114AB2 CRC64;
     MKTTVLIGLA ASFCFSFTAQ AQLRRLSQQQ TLGGQPSLTK PMNMLNGWSD DNHYIEMDQA
     ERKLYAVDLN TGERTPYTPP PKSNVNAFLK DNDVFIQYGK EAAKQLTSTK DEEKNPTLSP
     DGKYIAFTRN NDLYAVDVAT GQEVRYTNDG TDVIYNGWSS WVYFEEILGR PTQYKAFWWA
     PDSKRIAFMR FDDTKVPMFP INGSTGQHGY TEKTRYPKAG DPNPEVRVGF VPVTGGTVTW
     ADFNEKDDQY FGTPYWSYDG SSLMVQWMNR GQDNLKFFSV NPATGSKKEI YDEKQSSWVD
     LDYDGRIEYL QDKKHYILKS DKTGWAHFYL YTLDGKLINP ITSGKWQVTD LEHVDEKNKV
     IYFTARKEAS TRKDFYRVNY NGKSLKRLTF GDYTHQVQIS PNGKYFITTY SNVSTPQKRT
     LLDNTGKIIK ELGDSKSADF AQYNFGKTEM ITIPTDDGYQ LPAVITYPTD FDQNKKYPVI
     MSIYGGPNAG TVTNTWKGTA SQWWANEGII QIAVDHRASG QFGKEGVALM HRNLGKWEMK
     DYTTAARWLK AKSWVDNKKL LITGHSYGGY MTCMALTMGA DDFDFGIAGA PVTSWELYDS
     HYTERFMDTP QENPEGYKNG SVLTYVDKYK GLLRIMHGDM DDNVHMQNTI QLIDKLQNAN
     KHFELMIYPG GRHGWGGVKT PHDKAERIRF YYDHLLNKPV PADLLN
//