ID A0A2N3IIW3_9BACT Unreviewed; 697 AA.
AC A0A2N3IIW3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=Rain11_0757 {ECO:0000313|EMBL:PKQ70236.1};
OS Raineya orbicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ70236.1, ECO:0000313|Proteomes:UP000233387};
RN [1] {ECO:0000313|EMBL:PKQ70236.1, ECO:0000313|Proteomes:UP000233387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ70236.1,
RC ECO:0000313|Proteomes:UP000233387};
RA Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL Submitted (JUN-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:PKQ70236.1}.
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; NKXO01000009; PKQ70236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3IIW3; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000233387; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:PKQ70236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233387}.
FT DOMAIN 24..420
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 480..693
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 697 AA; 79640 MW; 6E13E7D8506CB982 CRC64;
MLRYYISTFL ISVSPMFAQK ISYPQTAKVN QIDEYFGVKV ADPYRWLEVS DSAAVKEWIK
AQNAVTFDYL SQIPYRNQIR KRLQEVWNYP KMGVPVSYGD FEIIQKNDGL QNQFVFYIKK
GTQEELLLDP NKMSAEGIVS INSWSVSENK RYFAYAWAKG GSDWNTIEII DLQTKQKLSE
KLEWVKFSGI AWYRDGFFYS RYDAPKAGKE YEAKNEFHKL YYHKIGTPQS QDELIFVDRK
NPLQNVSASV SEKNDLLYVF LPKGTAGTAI LYKKLTSFAD LKPLIAHQEA ENQLITTLDN
HAVIRTNYQA PRYRVVAVPL ENPAVENWKT LIPEAENVLT SVRYMNGYFI ATYMQDASHR
VWLFDKNGKK TNEIKLPALG TVAGFTGKEE ATFTYYTFSS FLQGGNIYKY DFITHTSTLY
FVPKIPFKAE NYETREVFYP SKDGKKVHLF ITHKKGLKRN GKNPTYLYGY GGFNISINPS
FDVRLIPFLE AGGVYAVANL RGGSEYGEEW HLDGARLKKQ NVFDDFIAAA EFLIKEKYTS
SEKLAISGRS NGGLLVGACM TQRPDLFAVA LPGVGVMDML RFHKFTIGWA WVPEYGSAEQ
SKEDFENLYK YSPLHNIKPA SYPATLVYTA DKDDRVVPAH SFKFIATLQE KQKGAKPTLI
RIDVDAGHGA GKPISKQIDE WADIWAFTLW NLGIKKM
//
