ID   A0A1I6LER9_9SPHN        Unreviewed;       709 AA.
AC   A0A1I6LER9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   ORFNames=SAMN05192580_2657 {ECO:0000313|EMBL:SFS01955.1};
OS   Sphingomonas jatrophae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1166337 {ECO:0000313|EMBL:SFS01955.1, ECO:0000313|Proteomes:UP000198824};
RN   [1] {ECO:0000313|EMBL:SFS01955.1, ECO:0000313|Proteomes:UP000198824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-249 {ECO:0000313|EMBL:SFS01955.1,
RC   ECO:0000313|Proteomes:UP000198824};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOZG01000002; SFS01955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LER9; -.
DR   STRING; 1166337.SAMN05192580_2657; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000198824; 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: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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198824};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..709
FT                   /note="prolyl oligopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011493712"
FT   DOMAIN          24..427
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          487..698
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   709 AA;  77655 MW;  DEE337ED5E3EC13E CRC64;
     MRFLLPFLLL GSAMSATAAP LSYPATEKGA VVDQSFGQAV PDPYRWLEND VRVDPKVRAW
     VTAQNQLTQS YLATLPGRDA IEKRLTALWN YERFGVPRKK GGRYFYTRNA GLQNQSVLYV
     RDTLDGQGRV LLDPNGWSAD GATALAEWEP SEDGSKLLYA IQDGGTDWRI IKVLDVATGK
     TLSDEVRWSK FGGGEWAKDG SGFYYSRFDA PAEGATFQAT NLNQKVYFHR LGTPQSEDRL
     VYATPDHPTW GHHATVSDDG RWLVISTNEG TDPRNDVTVI DLKQPSAKPR LLFTGLKNEW
     SFLGSTDSRL IFATDSDAPM RRIVAVDTSD ATPRPVQIVG EDKVKLESVR IAGNAIVADY
     LVDAKSELRL FDLAGKRLKD VPLAGVGSVL ATSGDMGERE AFFAFASFNR PTTIYRLDTT
     TGQATTFAAP KVAFNPDDYV VEQRFVPSKD GTKVPLFVVH KKGLDLSKGA PTLLYAYGGF
     DISMTPAFSP SNLAWMDMGG VYAQASLRGG GEYGRAWHDA GRLAKKQNVF DDMIASGEYL
     KREKIASALV VRGGSNGGLL VGAVVNQRPD LWAAALPAVG VMDMLRFDRF TAGRYWVDDY
     GYPTKEADWR VLRTYSPYHN IAAGKDYPAI LVTTADTDDR VVPGHSFKYT AALQAAQIGN
     KPHLIRIETR AGHGSGKPTS KLIEETADQW AFAAKWSGLA LPAEGTAAK
//