ID A0A3M0AC57_9GAMM Unreviewed; 707 AA.
AC A0A3M0AC57;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=DFR27_1381 {ECO:0000313|EMBL:RMA80025.1};
OS Umboniibacter marinipuniceus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Umboniibacter.
OX NCBI_TaxID=569599 {ECO:0000313|EMBL:RMA80025.1, ECO:0000313|Proteomes:UP000267187};
RN [1] {ECO:0000313|EMBL:RMA80025.1, ECO:0000313|Proteomes:UP000267187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25080 {ECO:0000313|EMBL:RMA80025.1,
RC ECO:0000313|Proteomes:UP000267187};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-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:RMA80025.1}.
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DR EMBL; REFJ01000003; RMA80025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0AC57; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000267187; 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:UP000267187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..707
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018195107"
FT DOMAIN 28..427
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 485..700
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 707 AA; 77819 MW; 853C2826D90F7635 CRC64;
MKKTAIGLAL LAFVGCTSNS NNSTIEYPVT AKGDVVDTYF GHQIADPYRW LEDDMSEETA
DWVQAENEVT FSYLNQIPFR QELKDRLTEL WNYEKVGAPF TEGDYTYWYQ NDGLQNQYVL
WRQKGESEAE IFLDPNQFSE DGTTSLAQVS FSDDGSLVAY SISEGGSDWR KIIVIDAETK
QPIEDTLVDV KFSGISWLGN EGFYYSSYDK PDGSELSAKT DQHKLYYHQL GTSQSNDPVI
FGGSEAEKHR YVGGGVSDDN RFLFISASVS TSGNKLFMLD LSDPEAELVT ILDDTRSDTY
VIDNDGAKLY LVTNLDAPNK RIVTVDASNP TPENWVDFIA ETDNVLSPST GSGYFFAEYM
VDAISQVKQY DYAGNFIRDI ELPGLGSVGG FSAKDDATTI YYSFTNYNTP GTTYSFEPHQ
GVSDVYRASG IEFDASDYVS EQVFYTSKDG TEVPMIITHK RGIELDGTNP TILYGYGGFN
ISLTPSFSVA NAVWLEQGGV YAVANLRGGG EYGKEWHDAG TQLQKQNVFD DFIAAAEYLN
TAGYANSDHL AIRGGSNGGL LVGAVMTQRP DLMKVALPAV GVLDMLRYHT FTAGAGWAYD
YGTAEQSEEM FKYLLGYSPV HNVKEGIPYP ATLITTGDHD DRVVPAHSFK FAAELQAKQG
GTNPVLIRIE TNAGHGAGTP VSKTIEQYAD IFGFTLFNMG VTELSAD
//