ID A0A0E3Z1V2_9GAMM Unreviewed; 721 AA.
AC A0A0E3Z1V2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=WQ53_09505 {ECO:0000313|EMBL:AKC86953.1};
OS Pseudoxanthomonas suwonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC86953.1, ECO:0000313|Proteomes:UP000033067};
RN [1] {ECO:0000313|EMBL:AKC86953.1, ECO:0000313|Proteomes:UP000033067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J1 {ECO:0000313|EMBL:AKC86953.1,
RC ECO:0000313|Proteomes:UP000033067};
RX PubMed=26067962;
RA Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL Genome Announc. 3:e00614-15(2015).
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}.
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DR EMBL; CP011144; AKC86953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3Z1V2; -.
DR KEGG; psuw:WQ53_09505; -.
DR PATRIC; fig|314722.6.peg.2040; -.
DR Proteomes; UP000033067; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000033067}.
FT DOMAIN 14..426
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 501..706
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 721 AA; 78545 MW; F33A7B1312823302 CRC64;
MPGCARAWAT DAPPPAKKIP VVDTYHGVEI VDPYRWLEDL RDPDTRDWIK AQAEYTDRVL
QALPERDAIL ARLQAPDAPE TVIRRVQRRG ERWFYLRRAP DENDFVLVMR ERAGPPERVL
VDPATAFADG RRWSINHFDA SPDGRHVAYL VSEGGREDPD TRVFDVQAGR DTGLRIERTW
DARWLPDGSG FFSMRLPRLS ESDSALDGRR NLRTYLHRLG APDPERDRLL AGAGIDPRLP
MDPIESATLT VPEGTELLLA RIDRGVDRHS AFYVAPLASL EEDAGIPWRR LADFQDEVAD
IAIHGQDLYL LSSRDAPRYR VLRTSLQAPD PARAQVVVAE GRGAIQAIAA ARDALYVQTL
DGGLSQLSRV EYGRGTPQPV ALPEGTSAAL LPRATAADAA GAVYALAAFT TPPAYLHYDP
AVGRSTDLHL LPPPTADRSR IQTRVLQAPS HDGVDVPMVV MHRKGIALDG SHPALLIGYG
AYGISILDPA NWPERSVIDR WVDNGFVLAI AGVRGGGEYG RPWHLAGKEA TKPNTWKDFI
AAAETLVREG YTRPERLAGN GASAGGILIG NAFVERPDLF AVALVDVGWT NALRLEASTN
GAGNAPEFGT TASRLGFEAL RAMDAFHKVK DGDRYPAVLL VHGYNDPRVD VWFSAKFAAR
LQAASGSGKP VLLRVDYDAG HGHGTGRAQN DAQDADKIAF IRWRLGLSGD AAARASGAAG
E
//
