ID   DPP7_PHOV8              Reviewed;         721 AA.
AC   A6L2J8;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
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; OrderedLocusNames=BVU_2253 {ECO:0000312|EMBL:ABR39912.1};
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
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 Leu-Arg-MCA, while
CC       this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-
CC       Pro-MCA. {ECO:0000269|PubMed:23246913}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR   EMBL; CP000139; ABR39912.1; -; Genomic_DNA.
DR   RefSeq; WP_011965538.1; NC_009614.1.
DR   AlphaFoldDB; A6L2J8; -.
DR   SMR; A6L2J8; -.
DR   STRING; 435590.BVU_2253; -.
DR   MEROPS; S46.002; -.
DR   PRIDE; A6L2J8; -.
DR   EnsemblBacteria; ABR39912; ABR39912; BVU_2253.
DR   GeneID; 66751082; -.
DR   KEGG; bvu:BVU_2253; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   OMA; PGRTNRW; -.
DR   OrthoDB; 99817at2; -.
DR   BioCyc; BVUL435590:G1G59-2344-MON; -.
DR   Proteomes; UP000002861; 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   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; Reference proteome; Serine protease;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..721
FT                   /note="Dipeptidyl-peptidase 7"
FT                   /id="PRO_5002698792"
FT   ACT_SITE        87
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        228
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        656
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   SITE            674
FT                   /note="Critical for substrate specificity of DPP7"
FT                   /evidence="ECO:0000250|UniProtKB:B2RKV3"
SQ   SEQUENCE   721 AA;  81212 MW;  6024AF4434BB5202 CRC64;
     MKKFKLLLLA LMCVAFLPSK ADEGMWLLQL MQEQHLADRM KAQGLLLEAD DIYNPNRVSL
     KDAVGIFGGG CTGEIISPDG LILTNHHCGY GAIQQHSSVE HDYLTDGFWA KSRKEELPTP
     GLKFKFVERI VDVTDKVNNK VKSGEVKEEE TFEYDFLKKL ADEELKASDL NGKAGISAQA
     LPFYAGNKFY LIYLKTYSDV RMVAAPPSSI GKFGGETDNW MWPRHTCDFS VFRIYADANG
     EPAEYNENNV PLKAKKHLAI SLKGINEGDY AMIMGFPGST NRYLTQSEVK QRMHSTNEPR
     IRIRGVRQDV LKKEMAASDK VRIQYASKYA GSSNYWKNSI GMNKAIIDNK VLETKAEQEA
     KFAAFAKAKG NTDYEKVVSE IDAAIEKSNP ILYNYTCFRE VFQGGIEFGT PYLILDKLKD
     AIKNKDKEAI NKNIETLKKV YADIHNKDYD HEVDRKVAKA LLPLYAEMVP ADALPAFYTT
     IQKDFKGNYD AYVDHCYDNS IFSNEANFNK FIKKPTVKAI EKDPMTAYVR AKYDLMDKLG
     NELAESMKGM DLLHKTYVRG LCEMYSPEPK APDANFTIRL TYGNVKSYNP KDGVHYKYYT
     TLKGVMEKED PTNPEFVVPA KLKELYEAKD FGRYALPNGD MPACFLTTND ITGGNSGSPV
     INGNGELIGA AFDGNWESLS GDINFDNNLQ RCIAVDIRYV LFIIDKLGGC KHLIDEMTIV
     E