ID   DPP7_CAPGI              Reviewed;         715 AA.
AC   C2M262;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Dipeptidyl-peptidase 7 {ECO:0000303|PubMed:23246913};
DE            Short=DPP7 {ECO:0000303|PubMed:23246913};
DE            EC=3.4.14.- {ECO:0000269|PubMed:23246913};
DE   Flags: Precursor;
GN   Name=dpp7; ORFNames=CAPGI0001_0817 {ECO:0000312|EMBL:EEK15537.1};
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. Most potently cleaves the synthetic substrate Met-Leu-
CC       methylcoumaryl-7-amide (Met-Leu-MCA), followed by Lys-Ala-, Leu-Arg- >
CC       Leu-Asp-, Leu-Glu-, >Leu-Lys, and >Val-Arg-MCA, while this enzyme does
CC       not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-Pro-MCA.
CC       {ECO:0000269|PubMed:23246913}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR   EMBL; ACLQ01000003; EEK15537.1; -; Genomic_DNA.
DR   RefSeq; WP_002665659.1; NZ_ACLQ01000003.1.
DR   AlphaFoldDB; C2M262; -.
DR   SMR; C2M262; -.
DR   STRING; 553178.CAPGI0001_0817; -.
DR   MEROPS; S46.002; -.
DR   PRIDE; C2M262; -.
DR   EnsemblBacteria; EEK15537; EEK15537; CAPGI0001_0817.
DR   eggNOG; COG3591; Bacteria.
DR   OMA; PGRTNRW; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..715
FT                   /note="Dipeptidyl-peptidase 7"
FT                   /id="PRO_0000435485"
FT   ACT_SITE        87
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        650
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   SITE            668
FT                   /note="Critical for substrate specificity of DPP7"
FT                   /evidence="ECO:0000250|UniProtKB:B2RKV3"
SQ   SEQUENCE   715 AA;  82061 MW;  F4A614B3A602A8F8 CRC64;
     MRKLIFSLVT SFFLLLPSVI RADEGMWFLM FIKRLNERDM QKKGLQLTAE EIYSINNNSL
     KNAIVQFNGG CTASIISPDG LVITNHHCGY GAIAGLSTPE HNYLKDGYWA KDRSQELPPK
     SLYVRFFVRM DNVTDRMLSV VNSSMSEKER QDALNREMEK IQKENSEGGK YVVSVRPFFQ
     GNEYYYFVYQ DFKDVRFVGT PPENVGKFGG DTDNWEWPRH TGDFSVFRVY TDKDGNPAPY
     SPNNIPMKAK KYLNVTLKGV QENDFAMILG YPGRTNRWVS SHWVDQQVKY GYPAWVEASK
     TAMDAMKAHM DKDKAVRLKY ASRYASLANY WKNRQGMIDA LTAHKTADLK RAAEKKFAVW
     ANKPENKAEY GNVLSDLATY FEKTNQEAAN HNYLLLFFRA SRIVPQANGY VKQLNTYLNS
     SSDQEKQQIR ERIAKELDAY YSESYLPAEI DLFADNLKLY ADKATDIPQE IAQIKSQYNG
     DFRKFAAEVF ARSIFTTKEN FENFMNNPSS DALQSDPIAQ IARVMIDKYY NSQSEALKDG
     YEKAFRKYVK GMRDSKVSLI LYPDANSTLR LTYGSVKSLP KDKRNHDVKR NYYTTFKTML
     EKYKPGDAEF DMPKKFVEMY EKKDFGRYLD KDGTMHVCFL TNNDITGGNS GSPVMNGKGE
     LIGLAFDGNI EAMAGDVIFD KKLQRTIVVD IRYVLWCIDT FGGAKHIVDE MTIIQ