ID L7W4D1_NONDD Unreviewed; 720 AA.
AC L7W4D1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN OrderedLocusNames=DDD_1328 {ECO:0000313|EMBL:AGC76455.1};
OS Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS dokdonensis).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC76455.1, ECO:0000313|Proteomes:UP000011173};
RN [1] {ECO:0000313|EMBL:AGC76455.1, ECO:0000313|Proteomes:UP000011173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17205 / KCTC 12402 / DSW-6
RC {ECO:0000313|Proteomes:UP000011173};
RX PubMed=23292138; DOI=10.1093/gbe/evs134;
RA Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA Kim J.F.;
RT "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL Genome Biol. Evol. 5:187-187(2013).
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; CP001397; AGC76455.1; -; Genomic_DNA.
DR RefSeq; WP_015361952.1; NC_020156.1.
DR AlphaFoldDB; L7W4D1; -.
DR STRING; 592029.DDD_1328; -.
DR KEGG; ndo:DDD_1328; -.
DR PATRIC; fig|592029.3.peg.1317; -.
DR eggNOG; COG1505; Bacteria.
DR HOGENOM; CLU_011290_1_1_10; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000011173; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AGC76455.1};
KW Protease {ECO:0000313|EMBL:AGC76455.1}.
FT DOMAIN 32..435
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 493..706
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 720 AA; 80636 MW; 9EA7868CFF43E770 CRC64;
MKKLFYGAAA LLVLISCKED EKKQVNMAMT YPQTKKVDTV DVYHGVEVAD PYRWLEDDRS
EETGEWVKSQ NKTTQEFLSQ ISYRDEIKDR LTNLWNYEKV GAPFIEGDYA YFYKNNGLQN
QYVIYRYLKD SDPETAEVFL DPNTFSKEGT TSLGGTSFTK DGSLFAYSIS EGGSDWRKII
VLDVNSMKQV GDTIVDVKFS GMSWKGNEGF YYSSYDKPDG SELSAMTDRH KLYYHKLGTP
QSEDEVIFGD NPNEKYRYVG GGVTDDQKYL VISGSTATNG GKLWMKELNV KNAPLVAVVD
NFDTNTYLIH NEGSKLWLVT DYNAPNRRII TTDFSNPAQD TWKDVIPETE HVLSPSTGGG
YIFTEYMVDA VSQVKQYDYN GELVREVKLP GIGNVGGFGA KEEDETLYYS FTNYTTPGST
YLYNIKEGTS ELYRKPNIKF NSEDYESKQV FYTSKDGTQI PMIISYKKGI ALNGKNPTIL
YGYGGFNISL NPGFSVTRAA WMEMGGVYAV ANLRGGGEYG KKWHDAGTKM QKQNVFDDFI
AAGEWLKENK YTDTKHLAIQ GGSNGGLLVG ATMTQRPDLA GVAFPAVGVL DMLRYNKFTS
GAGWSYDYGT AEDSPEMFEY LKGYSPLHNI EEGVSYPATM VTTGDHDDRV VPAHSFKFAA
ELQEKQAGDA PTLIRIETDA GHGAGKSTEQ QIQEWTDIYG FGLYNMGYEQ LPEASAKVKM
//
