ID A0A031JUE3_9SPHN Unreviewed; 731 AA.
AC A0A031JUE3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=BV97_03500 {ECO:0000313|EMBL:EZP80413.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP80413.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP80413.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP80413.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) 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 -!- 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:EZP80413.1}.
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DR EMBL; JFYZ01000017; EZP80413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A031JUE3; -.
DR STRING; 158500.BES08_09130; -.
DR PATRIC; fig|158500.4.peg.3570; -.
DR eggNOG; COG1505; Bacteria.
DR Proteomes; UP000024329; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..731
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001551914"
FT DOMAIN 32..437
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 498..711
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 731 AA; 80578 MW; F44C42A0089BF563 CRC64;
MKTSGLQVLA ALLLSGAATP IWAGPMSDIS YPQTRRDTVV ETQFGEAIAD PYRWLEDDVR
HSSEVADWVS RENAVTEDYL TALPQRAQFQ RRIRAFMDYE RFGIPVKAGG SYFYTRNTGL
QNQAQLFVRK GLDGKPRLLL DPNAWAKDGA TALDSWEPSQ KGRYLLYSVQ DGGSDWRILR
VIDVKTGEPL QDEVRWAKFT GLSWVGEEGF LYSRFPEPKE GAAFQSLNYN QAVYFHRIGT
AQDADELVYA TPDAPDRGHV ADVTQDGRLA LITSHVGTDA RYEVRVIDLD KRKRDGWKAV
PLVSGFTDDW KLVEGAGRKL WYVTNRDAPR YRLVGIDLDA PKAEWTEIVA EREDILERAG
IVGDRLVLNY MRDAASHAEI LALDGSVGKT LSLNGIGTAS GFRGKPGDPE TFYAFTSFNC
PASIYRMDLA TGVTTPFATP KMCYDPGAYV VEQRFFTSKD GTRVPMFIVR SRVVAKAKQP
VPTLLYGYGG FDVSLTPGFS ATRMAWLEAG GAFALANLRG GGEYGRAWHD AGRRQNKQNV
FDDFIAAGEF LVSEGIAKKD GLAIQGGSNG GLLVGAVVNQ RPDLFAAAVA QVGVMDMLRF
DRFTAGRYWT DDYGRPDRED DFKVLRAYSP YHNIREGAQY PAILVTTADT DDRVVPGHSF
KYTAALQHAN LGARPRLIRI ETRAGHGSGK PTDKAIEEGA DILAFVAQWT GLRLPAEASV
AQAGEPTAAT P
//
