ID A0A264Y8U1_9BACT Unreviewed; 740 AA.
AC A0A264Y8U1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=S9 family peptidase {ECO:0000313|EMBL:OZT04515.1};
GN ORFNames=CHL74_04930 {ECO:0000313|EMBL:OZT04515.1};
OS Prevotella sp. 885.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2022527 {ECO:0000313|EMBL:OZT04515.1, ECO:0000313|Proteomes:UP000216632};
RN [1] {ECO:0000313|EMBL:OZT04515.1, ECO:0000313|Proteomes:UP000216632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=885 {ECO:0000313|EMBL:OZT04515.1,
RC ECO:0000313|Proteomes:UP000216632};
RA Efimov B.A., Chaplin A.V., Kochetkova T.O., Sokolova S.R., Ogneva L.V.,
RA Rebrikov D.V., Kondova I., Langermans J.A., Shkoporov A.N.;
RT "Description of Prevotella sp. 885 sp. nov., isolated from rhesus macaque
RT feces.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OZT04515.1}.
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DR EMBL; NOVE01000009; OZT04515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264Y8U1; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000216632; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000216632};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..740
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012876385"
FT DOMAIN 120..457
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 544..740
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 740 AA; 84407 MW; BF0418EDB938ADEA CRC64;
MKTKLISIAL FSLLASTPMS AQELKHFTLE DLNFGGTNFR DMQPQNKYCT WWGNQLVRLD
RNACYLVDKK TGKETELMTL AQFNQWAGPT KDIKARSLMG ASFPFAGKPV VMVQSGDVIY
MVDFKRHNLV DRMDMEDGEA VLELNTKSGA AAILKDDNLY VKKGDSKWQL SEDGSRDIVY
GQAVHRDEFG IRKGTYFSPD GEKLAFYRMD QSMVTDYPQV EIPDPVFTNM DEGESVIAKY
APSRYPMAGE TSHKVTVGVF DMKTGKTVYL KAGDPTDRYF TNIAWSPDGE SVYMFEVNRD
QNDCRLTCYS AKTGEKTAEL YRETDERYVE PQDPILFLPW DNTKFIMQTR KDGYKHLYLC
ALGKNGSRMA SNTVSLDVKQ LTSGEWEVME VLGFNAKRHE IVIASNEANP IQRNIFSVSV
DNGKRRLVDD NGKGWHNSVL SEDGTSLYDN YSTPDIPRNI AIVDIASGKK TSYFKAENPW
KGYDVPEYSC GTIKADDGKT DLYYRMVKPT NFDPNKKYPT IIYVYGGPHA HNVDARWNYC
SRGWETYMAQ KGYLLFILDN RGSEHRGKAF EQATFRQLGQ VEMKDQMTGV EYLKTLPYVD
ADKIGVHGWS FGGFMTISLM TNYPDVFKVG VAGGPVIDWR WYEVMYGERY MDTPQANPEG
YEKTSLINKA KDLKGRLQII TGYNDPTVVP QHCLSFLKEC IKVGTQPDFF VYPGEPHNMR
GHQSVHLHER ISRYFDDYLK
//