DPP11_FLAPJ
ID DPP11_FLAPJ Reviewed; 713 AA.
AC A6GWM2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Asp/Glu-specific dipeptidyl-peptidase {ECO:0000303|PubMed:23246913};
DE EC=3.4.14.- {ECO:0000269|PubMed:23246913};
DE AltName: Full=Dipeptidyl-peptidase 11 {ECO:0000303|PubMed:23246913};
DE Short=DPP11 {ECO:0000303|PubMed:23246913};
DE Flags: Precursor;
GN Name=dpp11; OrderedLocusNames=FP0382 {ECO:0000312|EMBL:CAL42495.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 49418 / JCM 8519;
RX PubMed=23246913; DOI=10.1016/j.biochi.2012.11.019;
RA Rouf S.M., Ohara-Nemoto Y., Hoshino T., Fujiwara T., Ono T., Nemoto T.K.;
RT "Discrimination based on Gly and Arg/Ser at position 673 between
RT dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in
RT pathogenic and environmental gram-negative bacteria.";
RL Biochimie 95:824-832(2013).
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. Shows a strict specificity for acidic residues (Asp or
CC Glu) in the P1 position, and has probably a hydrophobic residue
CC preference at the P2 position. Preferentially cleaves the synthetic
CC substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to
CC Leu-Glu-MCA. {ECO:0000269|PubMed:23246913}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR EMBL; AM398681; CAL42495.1; -; Genomic_DNA.
DR RefSeq; WP_011962553.1; NC_009613.3.
DR RefSeq; YP_001295313.1; NC_009613.3.
DR PDB; 5JXF; X-ray; 2.10 A; A/B/C/D=18-713.
DR PDBsum; 5JXF; -.
DR AlphaFoldDB; A6GWM2; -.
DR SMR; A6GWM2; -.
DR STRING; 402612.FP0382; -.
DR MEROPS; S46.002; -.
DR EnsemblBacteria; CAL42495; CAL42495; FP0382.
DR GeneID; 66551517; -.
DR KEGG; fps:FP0382; -.
DR PATRIC; fig|402612.5.peg.394; -.
DR eggNOG; COG4717; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OMA; KDWFFNP; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR PANTHER; PTHR38469; PTHR38469; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..713
FT /note="Asp/Glu-specific dipeptidyl-peptidase"
FT /id="PRO_5002698278"
FT ACT_SITE 83
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 644
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT SITE 662
FT /note="Is essential for the Asp/Glu P1 specificity of
FT DPP11; involved in the recognition of the Asp/Glu residue
FT at the P1 position of substrate peptides"
FT /evidence="ECO:0000250|UniProtKB:B2RID1"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 287..307
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 310..339
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 363..367
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 368..393
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 399..417
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 419..432
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 442..459
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 480..484
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 501..510
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 512..527
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 529..553
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 568..574
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 591..597
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 655..662
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 667..671
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:5JXF"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 685..693
FT /evidence="ECO:0007829|PDB:5JXF"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:5JXF"
FT HELIX 699..703
FT /evidence="ECO:0007829|PDB:5JXF"
SQ SEQUENCE 713 AA; 80756 MW; 7F7D39210383E2D8 CRC64;
MKYLKLFLLL FIIQTQAQQG GMWIPSLLSG MNETEMKNLG MKISADDIYS VNHSSLKDAV
PHFNGGCTSE VISPKGLILT NHHCGFDAIQ NHSSVDHDYL TNGFWAMKME DELPNENLVV
TFIVSINDVT AQVLDGVASI TSETEKQNKI QENITKVTAS FAKEAWQENK VRTFFEGNQY
ILFVTEVFKD VRLVGAPPSL IGKFGSDTDN WVWPRHTGDF SMFRVYANKN NHPAAYSKDN
VPYIPKHFLP VSLDGVQEDD FTMVMGYPGK TQEYLPSFAV AQIVNETNPA KIEIREAALK
VQDGFMRKDN AIKIQYASKY AGVANYWKKW IGESQGLKKS NAIGLKQNFE KDFQQKVIAA
GKQNEYGNLL ADFQKYYTEI TPYAVSRDYF NEVVVKNTEL LSLGYKLYQL EQVFITKGEQ
AFNDRKENLI KSQADFFKDF NATVDEKVFE QLVALYATKA PKEFLPISLL NVEYKKFAPS
IYSKSKLVDY ANFKALLSGD AKAVLKKISL DKGYAFVKSL ADNYSKNIAP RYDEINLKIN
ALQRIYMKAQ LELYPNSRIF PDANSTLRVT YGKVKGYSPK DAIYYNPTTY LDGAIEKYIP
GDYEFDVPKK LIDLYNNKDY GQYGENGKLP VCFIGTNHTT GGNSGSPAVD AQGNLIGLNF
DRVWEGTMSD IHYDPSICRN VMVDMRYVLF IVDKFAGAKH LINEMKLVHP KKK
