ID   A0A2A3LJF3_9GAMM        Unreviewed;       713 AA.
AC   A0A2A3LJF3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Oligopeptidase B {ECO:0000313|EMBL:PBJ82986.1};
GN   ORFNames=CMZ84_12360 {ECO:0000313|EMBL:PBJ82986.1};
OS   Xanthomonadaceae bacterium NML93-0399.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae.
OX   NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ82986.1, ECO:0000313|Proteomes:UP000218035};
RN   [1] {ECO:0000313|EMBL:PBJ82986.1, ECO:0000313|Proteomes:UP000218035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ82986.1,
RC   ECO:0000313|Proteomes:UP000218035};
RA   Bernier A.-M., Bernard K.;
RT   "Clinical and environmental strains of Xanthomonadaceae.";
RL   Submitted (SEP-2017) 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:PBJ82986.1}.
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DR   EMBL; NTJI01000002; PBJ82986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3LJF3; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000218035; Unassembled WGS sequence.
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; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE   4: Predicted;
FT   DOMAIN          16..432
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          490..705
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  79937 MW;  362DF5E6A4291A4B CRC64;
     MMSVSPAATA ATPVPPDAEQ RPHTVEAPHG AKREDVYYWL RDDKREDPAM LAYLNAENAY
     ADAMLAALKP VEDRLYDEIV GRIQQDDSSV PYRDRGYWYY SRFETGKDYP VHARRADGTG
     VDALSIQAAN AKGDFSGEEV LLDVNQLAEG KDYYAVGDWD ITRDNRILAY ADDTNGRRQY
     TVRFKNLETG EVYPDVITGV SANLVWADDN RTLFYVENDP ETLLTVRVKK HVLGTPVADD
     VLVYEEKDDS FYMGIDRTRD EKYIVIGVGS TVSSETRYAP ADNPETFTVL APRARDVEYD
     ADHYGDRWVI RTNADKATNF KLVTAPSNAT SRTQWTDLVP HRDDVYIEGY ELFEGFTAIE
     ERAEALTRVR VLKADGSDEF MQADEPAYAM GLSINSEPDT AWLRYGYTSL TTPATTFEVN
     TQTGERRQLK QQAVIGYDPS NYVTERVWST ARDGTRVPVS LVYRKGFEKN GTAALLQYGY
     GSYGSSMDPG FSVTNVSLLD RGMVYAIAHI RGGEEMGRAW YDDGKLLNKV NTFTDFIDVT
     DDLVQKGYAA PDRVAAYGGS AGGLLMGAIS NMAPEKYRVI LSQVPFVDVV TTMLDPSIPL
     TTNEYDEWGN PEDKRYYDYI LGYSPYDNLE AKAYPAMFVG TGLWDSQVQY WEPAKYVAKL
     RDLNTGDHPV VFRTNMEAGH GGKSGRFRRY RESAEMYAFM LEQLGLGATQ AGG
//