ID   DPP11_CAPGI             Reviewed;         712 AA.
AC   C2M741;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
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; ORFNames=CAPGI0001_1068 {ECO:0000312|EMBL:EEK13929.1};
OS   Capnocytophaga gingivalis.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=553178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 / 27;
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 / 27;
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; ACLQ01000023; EEK13929.1; -; Genomic_DNA.
DR   RefSeq; WP_002669328.1; NZ_ACLQ01000023.1.
DR   AlphaFoldDB; C2M741; -.
DR   SMR; C2M741; -.
DR   STRING; 553178.CAPGI0001_1068; -.
DR   MEROPS; S46.002; -.
DR   EnsemblBacteria; EEK13929; EEK13929; CAPGI0001_1068.
DR   eggNOG; COG4717; Bacteria.
DR   OMA; KDWFFNP; -.
DR   OrthoDB; 99817at2; -.
DR   Proteomes; UP000003622; Unassembled WGS sequence.
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   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   PANTHER; PTHR38469; PTHR38469; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Hydrolase; Protease; Serine protease; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..712
FT                   /note="Asp/Glu-specific dipeptidyl-peptidase"
FT                   /id="PRO_0000435486"
FT   ACT_SITE        84
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        220
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        647
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   SITE            665
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"
SQ   SEQUENCE   712 AA;  80432 MW;  CAF2CAFB57746F5C CRC64;
     MKRFFKMALF LGVSALYGQQ GGMWIPSLLE GMNAKEMKTL GMKMTVADIY SVNKSSLKDA
     APHFNGGCSS EVISDKGLLL TNHHCGYGQI QAHSTLQNDY LANGFWAKSL AEELPNKNLK
     VTFMVRIDDV TKQVLKGTES ITDETEKAKL IEKNIAEVIK TAPKEAWQEN SVKAFYDGNQ
     YILFVTETFK DVRLVGAPPS SIGKFGSDTD NWVWPRHTGD FSLFRIYADK NNRPAEYSKD
     NVPYKPKHFF PISLKGVKEG DFVLVFGYPG TTQEYLPSAA VAQIENVINP ARIGIRDIVL
     KVQDSYMRKD QGIKIKYAAK YARVANYWKK WMGETKGLKK SGAVALKQQQ EAKFQQAIQK
     ANKQAQYGNL LSDFNRLYKE IEPYTLAANL NSEFIFRNID LLSNGSRLLQ LEKALEDKGE
     QSFNDRKKNL LNTFKEIFKD NDKQVDKDVF EKVVVFYAAN MPKNLLINSL KNFDAKKLAD
     NLYNNSFLTS LSGVESVLNL SAAEFKERMK NDVGIQFVRE LKEMNDTQVF PVYDRLNTQI
     HALQRTYMKA ILEFSKPSDR IFPDANGTLR VTYGKVAGFS PADAVTYSAH TTLDGVMEKY
     VPGDYEFDVP QHLRDLQAKK DFGRYGDKNG KMPLCFLSTC HTTGGNSGSP AIDANGNLIG
     LNFDRVWEGT MSDIHYDPKL CRNIMVDIRY VLFVIDKYAG AGHLVNEMKL IK