ID   A0A239DXZ7_9ACTN        Unreviewed;       691 AA.
AC   A0A239DXZ7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   ORFNames=SAMN06893096_103423 {ECO:0000313|EMBL:SNS37217.1};
OS   Geodermatophilus pulveris.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1564159 {ECO:0000313|EMBL:SNS37217.1, ECO:0000313|Proteomes:UP000198373};
RN   [1] {ECO:0000313|EMBL:SNS37217.1, ECO:0000313|Proteomes:UP000198373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46839 {ECO:0000313|EMBL:SNS37217.1,
RC   ECO:0000313|Proteomes:UP000198373};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FZOO01000003; SNS37217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239DXZ7; -.
DR   Proteomes; UP000198373; 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; IPR002471; Pept_S9_AS.
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:SF2; PROLYL ENDOPEPTIDASE; 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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          14..412
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          481..689
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   691 AA;  73453 MW;  A75D4BED7A6B029C CRC64;
     MGRVRHPSAE RLDLVEHLHG HAVADPYRWL EDPADPRTAS WTAAQDELTA GALAALPLRD
     RLAARLAELV HAGAVGVPVW RGGRAFSTRR DPGQEHAVLR VREPDGSTRV LVDPMAVDPA
     GTTTLDAWSP SWEGDRLAYQ VSTGGDEESR LYVLDVATGE QLDGPVDRCR YSPVAWLPGG
     EELFYVRRLA PDAVPVGEEQ FHRRVWRHRV GSDPDGDVLV HGEGLDLTNY YGVRTSRDGR
     WLSVSASAGT APRDDVWLAD LGGDGTLREL QVGVDAQTAA WVARDGRLWL MSDRGTPRWR
     LAVADPADPA TWAPGAWRDV VPEQAGGVLT DVALVDGPDG GLLVLAVHSV DATDRLSVWA
     ADGSGRVAEV SALPPGSVSG VSAPPEGGGT AWVGFTDHAT PPSVLRWDAA DPAALTTWEQ
     APVAGEVPAL RVVETHATSA DGTPVHLFVL SSDGVPGRPR PTVLYGYGGF NVALTPGYSA
     QALAWVAAGG VWAVANLRGG SEHGEEWHRA GMRERKQNVF DDFAAAGEHL VAEGWTTPAQ
     LAVMGGSNGG LLVGATLTQR PDLAAAVVCS APLLDMVRYE RFGLGRTWND EYGTADDPVE
     LGWLLGYSPY HRVVEGTAYP AVLFTTFESD TRVDPLHARK LAAALQHATS SGAPVLLRRE
     TSVGHGARAV SRTVALAADQ LAFLAAHTGL G
//