ID W4SI51_9XANT Unreviewed; 834 AA.
AC W4SI51;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Prolyl oligopeptidase-like protein {ECO:0000313|EMBL:GAE56196.1};
GN ORFNames=XPR_2831 {ECO:0000313|EMBL:GAE56196.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE56196.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE56196.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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:GAE56196.1}.
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DR EMBL; BAVC01000238; GAE56196.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SI51; -.
DR Proteomes; UP000019084; 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; 2.120.10.30; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..834
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004848201"
FT DOMAIN 658..822
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 199..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 90686 MW; 5D46F728B0ED4AC8 CRC64;
MLTAYRWSGL LVLASLLPVS AMAGTPDGGY RQPPEPLLSV LRAPLNPSPR LDPTGKTLLL
VQRTQYPPIA RVAEPYLKLA GVRVEPRTHS RHDMSNGYGI RSCLQGFSLV DLASGKQTAV
SLPAGACPAS PVWSPDGRRF AFNNTAADRV ELWVGEVATG NVRKIDGVQL NPVLGGEIQW
LGGSDTLLLK TVPQDLGAAP RKAAVPPGPE VKETIQGKGE SSTYEARDTL SSPEDEALFS
YYATSQLLTV DAATGSQRKL GSPAVYSNVD GAPDGRHVLV ERLKQPYSYV TTYARFAHDV
AVLDLANGNA RVLADLPVAD RVPVQGVPVG PRAYSWRANQ PATLVWAEAL DGGDWKTSVP
ARDKLMTLAA PFAAKPREVT RVQQRYAGLS WFAAGGQALL DEYDENRHWR RTTLLDADRP
GAAGRVLFDL STDDLYADPG VPETRTLSNG QAILREEQGA LFLSGQGASP AGDRPFLDRY
ELASGKTRRL FRSDASVDEV FFGFAGDDVA RLLTWHQSLT DPPNVYLRTL GQPLPTAATG
EAVLASTATP VTHFPDPTPL VRQIKKRLVT YKRKDGVELS FTLYMPPGYK DGTRVPAILY
AYPLDYADPS KAGQVSGASE RDFTRLRYYQ LLLLAGYAII DDAAFPIVGD PKTAYDTYLQ
QLVDDATAAV DKAVELGVVD RQRIGVTGHS HGALMTANLL AQTDLFRAGA ATSGSYNKTL
TPFGFQNERR SFWAAPEVYA QASAFFHADK INEPLLIVHG MDDANPGTET TQAPRLFQAI
RGNGGTARLV LLPFEPHWYT ALESTEDVVA EMLEWFDRYV KNAPPRDADN KPKQ
//