ID A0A420XNP5_9ACTN Unreviewed; 697 AA.
AC A0A420XNP5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-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=CLV35_2299 {ECO:0000313|EMBL:RKS73808.1};
OS Motilibacter peucedani.
OC Bacteria; Actinomycetota; Actinomycetes; Motilibacterales;
OC Motilibacteraceae; Motilibacter.
OX NCBI_TaxID=598650 {ECO:0000313|EMBL:RKS73808.1, ECO:0000313|Proteomes:UP000281955};
RN [1] {ECO:0000313|EMBL:RKS73808.1, ECO:0000313|Proteomes:UP000281955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP-AC37 {ECO:0000313|EMBL:RKS73808.1,
RC ECO:0000313|Proteomes:UP000281955};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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:RKS73808.1}.
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DR EMBL; RBWV01000012; RKS73808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420XNP5; -.
DR InParanoid; A0A420XNP5; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000281955; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000281955}.
FT DOMAIN 16..422
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 486..694
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 697 AA; 75031 MW; EE180B0164E8A8C5 CRC64;
MSRPDYPAAP RLDLVEQLPE SAPAHSVADP YRWLEDPADP AVEAWSSAQD VLVREHLDAL
PGREHVAERL RALLAAGSVG SPALRGDRRF FMRRTAEQEH AVLLVQEADG SERVLLDPMA
VDPSGKTTID SWQPSKEGRL LAYQLSEGGT EESVLRVLDA GTGELVDGPI DRARYSPVAW
LPGGEAFYYV RRVDPAGLPA EEQQYHRRVW LHRLGADPAD DVLVFGEGLE KTNYYGVSVS
MDGRWLTVSA SEGTAPRNDL WVADLGASSL EAPALQEVQV GVDAQTGVHF ARDGRAYVFT
DLDAPRGRLC VADPGELQVS GWTDLVPEDP EAVLDGYALL DGDELDEPVL LCSWTRHAVS
ELTAHRLADG GGARPVQLAG VGSLGGLSTH PEGGHEAFFG YTDHVTPSSV YRYDATDGSV
SLHASPPGSV EVPQVSVRLV PYTSKDGTTV RMFVVSPTEA PDRPRPTVLY GYGGFGIPMS
PGYSSGILQW VEAGGVYAVA CLRGGGEEGE QWHRDGMLGH KQNVFDDFHA AAETLVAEGW
TTPAQLGISG GSNGGLLVGA ALTQRPELYG AVVCSAPLLD MVRFEKFGLG ATWAVEYGSA
ADPEQLGWLL SYSPYHHVVD GVDYPATLFT VFDSDTRVDP LHARKLAAAL QHATSGERPV
LVRREKDVGH GARSLSRSID LSVDTTVFLA HWTGLQL
//
