ID G7US77_PSEUP Unreviewed; 794 AA.
AC G7US77;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dipeptidyl-peptidase {ECO:0000313|EMBL:AER54746.1};
GN OrderedLocusNames=DSC_00465 {ECO:0000313|EMBL:AER54746.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER54746.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER54746.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER54746.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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DR EMBL; CP003093; AER54746.1; -; Genomic_DNA.
DR RefSeq; WP_014162067.1; NC_016147.2.
DR AlphaFoldDB; G7US77; -.
DR STRING; 1045855.DSC_00465; -.
DR KEGG; psd:DSC_00465; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_019735_0_0_6; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000005870; Chromosome.
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:UP000005870};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..794
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003504325"
FT DOMAIN 337..503
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 596..791
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 794 AA; 88086 MW; 7C94978FFEBD5E30 CRC64;
MRLSAAVLSC LMLSPAAFAQ APASTPLTIE QVMADLDWIG PPVEDARWTW DSRAVEYALK
RNGSPIRDTF RQELSASAAT RVADDARHTL GAPGAVFDGK RQHQAFVRNG DVFVRNLRSG
ALTQLTRTLE EETAPQFGSD GALVWRVGNQ WWHWNGTSVA QAAQARAEDD PDKPKSEDLL
REQQLRTLST LAHDRDMRQA LRRQEDRWRK ADPSRAPAPV YLGSKVQIEQ TALSPDGQWL
LIVTQEKGAE AGRAGKVAHY VTESGYAEDQ EARTLVGRNS PVPQALWLAD MRTGTAKPLS
FDALPGITSD PLAGLRKAAG KEPIKGNRAV RVESDGDGSG AAIQWSADSR NVAVLLRATD
NKDRWIAGVD LANARLQVRD RLTDPGWINW SFNEFGWLAD NETLWLLSEA SGYSQLYTQR
GTERPRALTS GQWEASAPVP AADGDRFYFL CNRTAPGRYE VCQVDLKTGK VAEVTALDGG
VEGFSQSPDG RWLLVQYSAS YLPTQLAVVP ANGGAARVLT DTRTAAYKAQ PWIQPQLVQV
PSRHGAGTVW GKYYGPARTV PGKRYPIVMF VHGAGYLQNA IAGYPPYPRE QMFHNLLVQQ
GYLVLDLDYR GSAGYGRAWR TAIYRNMGHP ELDDYLDGLD WLIAHHQGDR DRAGIYGGSY
GGFMTYMALF RAPGVFKAGA ALRPVADWTQ YNHQYTSNIL NTPDLDPQAY RISSPIEYAD
GLQDRLLIAH GMIDDNVFFK DSVDMAQKLI ELHKDNWSLA PYPLERHSFT RADSWLDEYK
RVLDLFNDAL KPAP
//
