ID A0A2N0ES99_9FLAO Unreviewed; 720 AA.
AC A0A2N0ES99;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=ATE92_1125 {ECO:0000313|EMBL:PKA82981.1};
OS Ulvibacter sp. MAR_2010_11.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=1250229 {ECO:0000313|EMBL:PKA82981.1, ECO:0000313|Proteomes:UP000232889};
RN [1] {ECO:0000313|EMBL:PKA82981.1, ECO:0000313|Proteomes:UP000232889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_11 {ECO:0000313|EMBL:PKA82981.1,
RC ECO:0000313|Proteomes:UP000232889};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (NOV-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 -!- 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:PKA82981.1}.
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; PHTY01000001; PKA82981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0ES99; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000232889; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 31..434
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 491..706
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 720 AA; 80477 MW; 318E9F2DC7280D90 CRC64;
MKKLIIPFFI AFTLMACKEE LKKEPIAVTY PKTQKVDTVD NYFGVDVQDP YRWLEDDRSA
ETESWVKSQN EVTFGYLDKI PFRDELKERL SSLWNYEKVG PPFKEGDYTY FYKNDGLQNQ
FAVYRYKTGE DPATAEIFLD PNTFKEDGTI SMDGLSFSED GKLAAYSISD GGSDWRKVLV
MNTETKKIIE DTIVDVKFSG LSWKANEGFY YSSYDKPKGS ELSAKTDQHK LYYHKLGTKQ
KEDALIFGGI PAEKHRYVGG YVTDDNSYLV VTASVSTSGN KLFIKDLTKP NSKFVTVLNH
NDSDTNIIDN VGSKLYLVTN LNAPNKKIVT VDAANPTPEN WVDLIPETEN VLSANKAGGN
FFTEYMVDAV SKVLQYDYNG KLIREVQLPG IGSAGGFGAK KEEKELYYSF SNYVTPGTIY
KYNIASGKSE LFRKSTIDFN PEEYESKQVF YNSKDGTKIP MIITHKKGLK LDGKNPTILY
GYGGFNISLT PSFSITNAVW MEQGGIYAVP NLRGGGEYGK KWHDSGTKMQ KQNVFDDFIA
AAEYLIENKY TSSDYLAVRG GSNGGLLVGA AMTQRPDLMK VALPAVGVMD MLRYHTFTAG
AGWAYDYGTA EDNKEMFEYL KGYSPVHNVK AGVAYPATLI TTGDHDDRVV PAHSFKYAAE
LQEKQSGPNP VLIRVEVDAG HGAGTPVTKS IEQYADIFGF TLYNMGYEVL PEKINKGVKE
//
