ID A0A434AVD5_9BACT Unreviewed; 707 AA.
AC A0A434AVD5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=DLK05_07670 {ECO:0000313|EMBL:RUT78447.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT78447.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT78447.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT78447.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) 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:RUT78447.1}.
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DR EMBL; RJJX01000008; RUT78447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AVD5; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000282985; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282985}.
FT DOMAIN 28..426
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 487..699
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 707 AA; 80523 MW; 1D82206ADD7D5147 CRC64;
MEKIALLTLT CLMIGACSSP VSKMNYPLTK KVDTLDTYFD TKVQDPYRWL EDDNSTETKE
WVIAENNVTN NYLSKIPYRN KIKKRLTALW NYPKVGVPFK KGNLYFHYRN NGLQDQYVLY
VQNSLKDTAR ILLDPNQLSE DGTVALSGIA VSEDSKYLAY RIARSGSDWN ELYVRNIKTG
EDLNDHLMWL KFTGVAWYQN GFFYSRYNAP EEGGALSNSN EYHKIYYHKL GDSQENDQLI
YQNEKYPKRL YGATVTDDQK YLIISEMGAS NGNGLYFKDL TKKGSSIQLI TDDLQKKHSI
IDDVDGKFLM FTNEGAPKNR LVAVDINRPT KENWEEVIPE KENVLHDVNL AGGKIVASYM
KDAYSEIEIL NLNGKFESKL EMPGIGTVGS FSGKKEDKIA FYSYTSFTTP SIAYKYDFTI
GKSEIFYQPK INFDPDDFVT EQKFYTSKDG TKVPMFIVHK KGVKLDGSNP CLLYGYGGFD
ISLTPYFTPR RMVWLENGGV FALANLRGGG EYGEKWHTAG TKMNKQNVFD DCIAAAEYLI
KENYTNPEKL VLKGGSNGGL LVGAVINQRP DLFKVAIPEV GVMDMLRYNK FTIGWSWAGD
YGTSSDSKEM FDYLYAYSPI HNITEKIKYP AILVTTADHD DRVVPAHSFK YIATLQEKYH
GENPVLIRIE SKAGHGGGMP TSKQIEEYTD IWSFIFYNME LTPKFMK
//
