ID A0A095D6W5_9SPHN Unreviewed; 719 AA.
AC A0A095D6W5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=FG91_01587 {ECO:0000313|EMBL:KGB54958.1};
OS Sphingopyxis sp. LC81.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1502850 {ECO:0000313|EMBL:KGB54958.1, ECO:0000313|Proteomes:UP000029574};
RN [1] {ECO:0000313|EMBL:KGB54958.1, ECO:0000313|Proteomes:UP000029574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC81 {ECO:0000313|EMBL:KGB54958.1,
RC ECO:0000313|Proteomes:UP000029574};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) 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:KGB54958.1}.
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DR EMBL; JNFD01000014; KGB54958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095D6W5; -.
DR STRING; 1502850.FG91_01587; -.
DR PATRIC; fig|1502850.3.peg.1613; -.
DR eggNOG; COG1505; Bacteria.
DR Proteomes; UP000029574; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KGB54958.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..719
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001906099"
FT DOMAIN 40..444
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 503..715
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 719 AA; 78269 MW; 8FD79D5B739F3A49 CRC64;
MSRKALSTPL ALVALTMFPG AAAAADAAAT SATAKALTYP DTPRGDTVDP QFGVDVADPY
RWLEDDVRVN PKVADWVAAQ NKVTDTYLDT LPGRDSFKER MTELYNYERF GLPTKAGTRY
FYSRNDGLQP QSVLYVREGL KGEGRVLIDP NAWAKDGATA LGEWNPSEDG KHLLYSVQDG
GTDWRIVRVK DVATGQDLSD EVRWVKFSAL DWAKDGSGFY YSRFPEPEEG EAFQSLNENH
SVYFHKLGTP QSADVLIHAT PDKPKLNNSA VVTDDGQYLL VISSEGTDER YGLTLHPLGK
RGAKPITLVD DFANNWEYVT NEGPHFTFVT NKGAPRGRIV SMDIRKPAAL TQLVGENEAT
LVGASRVGNR LILSYLGDAK SEARMVALDG KPIANIKLAD IGAATGFGGK SSDPETFYSF
SSYARPTTIY RFDTATGKSE IFAEPKLTFK PADFSVEQRF YKSKDGTEVP MFLVMKKGLD
RSKGSPTLLY GYGGFNVSMT PGFSPTKLAW VDKGGVLAIA NLRGGGEYGK AWHDAGRLDK
KQNVFDDFIA AGEYLIAEGI AGKGQIAIEG GSNGGLLVGA VTNQRPDLFA AALPAVGVMD
MLRFDRFTAG RYWVDDYGYP SKEGDFKNLL AYSPYHNIKD GTAYPAVLVT TADTDDRVVP
GHSFKYTAAL QHAKAGDKPH LIRVETRAGH GSGKPTDKII AEAADKYAFA AKWTGLSVE
//
