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Database: UniProt
Entry: A0A0G0JEX2_9BACT
LinkDB: A0A0G0JEX2_9BACT
Original site: A0A0G0JEX2_9BACT 
ID   A0A0G0JEX2_9BACT        Unreviewed;       677 AA.
AC   A0A0G0JEX2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   ORFNames=US50_C0018G0007 {ECO:0000313|EMBL:KKQ35319.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWB1_37_5.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618742 {ECO:0000313|EMBL:KKQ35319.1, ECO:0000313|Proteomes:UP000033876};
RN   [1] {ECO:0000313|EMBL:KKQ35319.1, ECO:0000313|Proteomes:UP000033876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(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}.
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:KKQ35319.1}.
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DR   EMBL; LBTF01000018; KKQ35319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0JEX2; -.
DR   PATRIC; fig|1618742.3.peg.390; -.
DR   Proteomes; UP000033876; 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          4..398
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          462..674
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   677 AA;  77567 MW;  1536EE4EA439B921 CRC64;
     MKFPVTKKEN IVDELFGYKI FDPFRWLENG ENEDVKKWVE EQNSFAFSSL KGVEFDIFQK
     ELALNYKYTS FSNPVPVKGK YFYSERKPDE NQNVIYYKIG IDGELVKLVD PNILSKESTV
     AVDYWGISRS GKYLIYGLSE GGTEMATLHI KDVDKNSDLN EKIINCRYSS TAWLPDDSGF
     FYTRNPRPGT APKGEEHLHT KVYFHKIGDN PDNDEMIFGD GRPKDDMISI TISLDGRLLS
     ISASQNWIEN EIYIYDISKK NTKLLIKKMK AKFHLSFLKD KILIYTNYKA DNYRILQSSY
     EDMLLDIEKW KEFLPEEKSL LSGFNITEEK ILVEYLVNAS SKVKICDYNG KHLGDIPLPE
     YSSLSGISTR KTEKEFFYSV TSFTFPPVIY RYIPDEDKYL EYNRIENPIN PDDYIIKQEW
     FLSSDGTKVP MFIFHRKELK QNGDNPTILY GYGGFASALT PSFSRGYMPW VNKGGIFVYA
     NIRGGSEFGK SWHLSAIKEN KQKSFDDFIA AAEHLIRNKY TSSRQLGVLG GSNGGLLVSV
     AAVQRPDLFG AVVSNVPLTD MVRFHKFGIA ARWVHEYGNP ETKEELENIL KWSPYHNIKD
     GIRYPNFLFV TGEKDSRVDP LHSRKMAALL QSVVKDNNVL LFTETEAGHG AGKPIYKIVE
     AQALKITFLA KYLGLSI
//
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