ID   DPP7_BACFN              Reviewed;         721 AA.
AC   Q5LB17;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BF9343_2924 {ECO:0000312|EMBL:CAH08705.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow
RC   {ECO:0000312|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
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-, and to a
CC       much lesser extent Lys-Ala-, Leu-Asp-, Leu-Glu-, Leu-Lys, and Val-Arg-
CC       MCA, while this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-,
CC       or Gly-Pro-MCA. {ECO:0000269|PubMed:23246913}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR   EMBL; CR626927; CAH08705.1; -; Genomic_DNA.
DR   RefSeq; WP_005789096.1; NZ_UFTH01000001.1.
DR   AlphaFoldDB; Q5LB17; -.
DR   SMR; Q5LB17; -.
DR   STRING; 272559.BF9343_2924; -.
DR   MEROPS; S46.004; -.
DR   EnsemblBacteria; CAH08705; CAH08705; BF9343_2924.
DR   GeneID; 66332175; -.
DR   KEGG; bfs:BF9343_2924; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   OMA; PGRTNRW; -.
DR   Proteomes; UP000006731; 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_5004259436"
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;  81134 MW;  62027F77A37CB477 CRC64;
     MNRLKLYLLA LTALAVCSAK ADEGMWLLQL MQQQHSIDMM KKQGLKLEAQ DLYNPNGVSL
     KDAVGIFGGG CTGEIISPEG LILTNHHCGY ASIQQHSSVE HDYLTDGFWA TSRDKELPTP
     GLKFTFIERI EDITDIVNLR IAAKEITESE SFSSTFLNKL AKELFEKSDL KGKKGIVPQA
     LPFYAGNKFY MFYKKVYPDV RMVAAPPSSI GKFGGETDNW MWPRHTGDFS MFRIYADANG
     EPAEYSASNV PLKTKKHLNI SIKGLKEGDY AMIMGFPGST SRYLTVSEVK ERMEASNAPR
     IRIRGTRQDV LKEAMNASDK VRIQYANKYA GSSNYWKNSI GMNKAIIDNN VLGTKAEQEA
     KFAKFAKEKN NTDYMNVVAK IDEAVAKTSP IKYQQTCLTE TFFGGIEFGS PFMVMDKLKE
     ALEQKNDSSI EANIKVLKEV FNDIHNKDYD HEVDRKVAKA LLPLYAEMIP AGQRPAIYDV
     IEKEYKGDYN AYVDAMYDTS ILANQANFDK FIKKPTVKAI EKDIATQYSR AKFDKYTNLA
     EQMGKLPEEL ALLHKTYIRG LGEMKLPVPS YPDANFTIRL TYGNVKPYSP KDGVYYKYYT
     TTDGILEKEN PEDREFVVPA KLKELIEKKD FGRYALPNGE MPVCFLSTND ITGGNSGSPV
     LNENGELIGC AFDGNWESLS GDINFDNNLQ RCINLDIRYV LFILEKLGGC GHLINEMTIV
     E