ID   A0A023Y1V2_9GAMM        Unreviewed;       820 AA.
AC   A0A023Y1V2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:AHY58587.1};
GN   ORFNames=DX03_07805 {ECO:0000313|EMBL:AHY58587.1};
OS   Stenotrophomonas rhizophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY58587.1, ECO:0000313|Proteomes:UP000025222};
RN   [1] {ECO:0000313|EMBL:AHY58587.1, ECO:0000313|Proteomes:UP000025222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA   Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT   "Is there a border between beneficial and pathogenic bacteria?";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP007597; AHY58587.1; -; Genomic_DNA.
DR   RefSeq; WP_038687690.1; NZ_CP007597.1.
DR   AlphaFoldDB; A0A023Y1V2; -.
DR   STRING; 216778.DX03_07805; -.
DR   GeneID; 61475841; -.
DR   HOGENOM; CLU_017120_0_0_6; -.
DR   Proteomes; UP000025222; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..820
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001528001"
FT   DOMAIN          661..818
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          192..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  89177 MW;  585B7814B4E5C0C5 CRC64;
     MPIRRTSLAA AVAVATLSLF ATAPAFADYA KPPEHLLKVL KAPPPPAPSL DPSGQRLLLT
     TAQTYPSIER VAQPYLKLAG VRLEPKNRSR HDTQGGYGIP ACVADFTLVD VGTAKHTKVA
     LPQGCAGAAQ WSADGQRFAF QNAVDTSVQL WVGDAVTGQV KQVPDVQLNP IFGYTLQWLG
     GGQQLLVKRV PANQGPAPTS GNGPGGPDVQ ESLGSSGESS TYEARDTLTS AHDEKLFAYY
     GASQLAVVDV AAGQVRNVGT PALYNEVNAA PDGVHVLTGT LMAPFSHAVT YQRFANDVAV
     LDLATGRAAP IASLPLADRV PVHGVPEGPR DFDWRATDPA TLVYAEALDK GDWKVTVPHR
     DRVLALKAPF NGKPQEIART AQRFEGIAWS ADPAVSFLFE NDENRHWRQT RIVDVDQPTK
     EGRLLWDLSS DEQYADPGNL VFTRLPNGAS VVRQDGAFVF LRGQGASPQG DRPFLDRLDL
     GSLKTERLFR SDADAYEQIL GLTATPGRYL TWHQSVMDPP NAFVRQQGER NAAAKEGEAQ
     YASTATALTR LTDPTPEVRQ IQKRLVTYKR ADGVDLSFTL YTPPGYKEGQ RVPAILYAYP
     ADFASAAQAG QVSGSQQTFT RLAPYRLMLL AGYAIIDNAS FPIVGDPKNA YDTYLEQLEA
     DAKAAVDKAV DLGVVDRNRI GVTGHSHGGL MTANLIAHTT LFKAGVATSG SYNKTFTPFG
     FQNERRSVWQ AQDVYLKASP FFYADKIKLP LLLVHGEDDA NPGTEPFQSR KLYQAIRGNG
     GTTRLVMLPN EPHWYTALES NEQLVYEMLT WFDTYVKNAR
//