ID   A0A0Q4G5A5_9SPHN        Unreviewed;       687 AA.
AC   A0A0Q4G5A5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Prolyl oligopeptidase {ECO:0000313|EMBL:KQM73279.1};
GN   ORFNames=ASE72_01030 {ECO:0000313|EMBL:KQM73279.1};
OS   Sphingomonas sp. Leaf20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735685 {ECO:0000313|EMBL:KQM73279.1, ECO:0000313|Proteomes:UP000051642};
RN   [1] {ECO:0000313|Proteomes:UP000051642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQM73279.1}.
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DR   EMBL; LMKN01000001; KQM73279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4G5A5; -.
DR   STRING; 1735685.ASE72_01030; -.
DR   Proteomes; UP000051642; 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; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR42881:SF13; PROLYL ENDOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 2.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051642}.
FT   DOMAIN          6..239
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          321..403
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          481..682
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   687 AA;  75120 MW;  82BBEE21D2EFE71B CRC64;
     MTTPNASKAP QADAAADPYI WLEDKDGAKP LAWVEAENAV TLPRLQNDPR YKSFYAEALA
     IAAAKDRIPM PDQRFGRIYN FWRDAEHPQG IWRWTSEAGY AQATPVWTTA LDLDALSKAE
     GKKWVWKGAT CLQPDERLCL VSLSEGGEDA VTYREFDLQT GQFVPGGFTL PTSKQGASWV
     DKDTLLVARD WGAGSMTASG YPFVVKEVKR GQPLSAAREI FRGETSDQLG TYAGVMTDGQ
     GNRVTMIQRR PTFFGGEKHV VTPTGLVKLD VPARVFPSGM VDGHVIFSTS EAWGQIPAGA
     IASAPLDEVR KGRFTPTLIF APNARQSVDG VSVTRDHVVA SVYDNVRGRA MVFTRGKTGW
     TSRAVALPDN ASIDVASTTD RSNATFVQVT GFLQPTTLWT LDAGPTGVPK QVKALPAKFD
     ASNDIVEQFE AVSTDGTKIP YFVVHRKGVP LDGTTPTIMT AYGGFESSMT PYYSGVMGKL
     WLERGGSFVL ANIRGGGEFG PKWHDAGRKT KRQIIYDDFA AVGKDLIARK LTSTKTLGIY
     GGSNGGLLMG VEFNQHPDLW KAVTIQVPLL DMIRYEQIAA GASWVDEYGS VAVPEEKAFL
     ETISPYQNIK RGVAYPEPYI WTTTKDDRVG PQHARKFAAR LKEYGLPYLF YEDTAGGHSG
     DADIEQGARM QALQMTYFAQ KLMGPAK
//