ID   DPP7_POREA              Reviewed;         818 AA.
AC   C3JAQ3;
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=Dipeptidyl-peptidase 7 {ECO:0000303|PubMed:25494328};
DE            Short=DPP7 {ECO:0000303|PubMed:25494328};
DE            EC=3.4.14.- {ECO:0000269|PubMed:25494328};
DE   AltName: Full=MER278904 {ECO:0000303|PubMed:25494328};
DE   Flags: Precursor;
GN   Name=dpp7 {ECO:0000303|PubMed:25494328};
GN   ORFNames=POREN0001_0291 {ECO:0000312|EMBL:EEN82793.1};
OS   Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS   NCTC 13058 / HG 370).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=553175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370;
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   IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RC   STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370;
RX   PubMed=25494328; DOI=10.1371/journal.pone.0114221;
RA   Nishimata H., Ohara-Nemoto Y., Baba T.T., Hoshino T., Fujiwara T.,
RA   Shimoyama Y., Kimura S., Nemoto T.K.;
RT   "Identification of dipeptidyl-peptidase (DPP)5 and DPP7 in Porphyromonas
RT   endodontalis, distinct from those in Porphyromonas gingivalis.";
RL   PLoS ONE 9:E114221-E114221(2014).
CC   -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC       oligopeptides. Most efficiently cleaves the synthetic substrate Met-
CC       Leu-methylcoumaryl-7-amide (Met-Leu-MCA), and slowly hydrolyzes Leu-
CC       Gln-, Lys-Ala-, Leu-Arg, and Ala-Asn-MCA. Is likely involved in amino
CC       acid metabolism and bacterial growth/survival of asaccharolytic
CC       P.endodontalis, that utilizes amino acids from extracellular
CC       proteinaceous nutrients as energy and carbon sources.
CC       {ECO:0000269|PubMed:25494328}.
CC   -!- DOMAIN: The C-terminal Lys-rich domain (711-818) is dispensable for the
CC       proteolytic activity. {ECO:0000269|PubMed:25494328}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR   EMBL; ACNN01000020; EEN82793.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3JAQ3; -.
DR   SMR; C3JAQ3; -.
DR   STRING; 553175.POREN0001_0291; -.
DR   PRIDE; C3JAQ3; -.
DR   EnsemblBacteria; EEN82793; EEN82793; POREN0001_0291.
DR   eggNOG; COG3591; Bacteria.
DR   OMA; KDWFFNP; -.
DR   Proteomes; UP000004295; 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; Reference proteome; Serine protease;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..818
FT                   /note="Dipeptidyl-peptidase 7"
FT                   /id="PRO_5002928037"
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        645
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   SITE            663
FT                   /note="Critical for substrate specificity of DPP7"
FT                   /evidence="ECO:0000250|UniProtKB:B2RKV3"
SQ   SEQUENCE   818 AA;  91085 MW;  3247A5B2FA621FB3 CRC64;
     MKLKRILLSV ALLCGIGTTA MADKGMWLLN ELNQQNYERM KELGFKLSPE QLYSLGQPSV
     ASAVVIFGGG CTGITVSNEG LIFTNHHCGF GAIQSQSTVD HDYLRDGFRS NNHVEELPIP
     GLSVRYLREI VDVTPRIEAA VKGAKSEMER MQIIEELSQK INAEYTKGST VVGEVTPYYA
     GNKYYVVVYN VFQDVRLVMA PPSSVGKFGG DTDNWMWTRH TGDFSVFRVY ADANNNPALY
     SQNNKPYKPI SYAPVSLNGY REGDYAMTIG FPGSTNRYLT SWGVEDVVNN ENSPRIEVRG
     IKQAIWKEAM EADQATRIKY ASKYAQSSNY WKNSIGMNRG LKNLDVVNRK RAEEKAFEAW
     IAKNNSQSTY GHILPGLKAD YAKSAAISKD INYLYETLWG GTEIVRLARD VNSVGRIQAA
     DMPKYKGRLE ELYKDYLPSL DVKVLPAMLD IVRQRVSADC QPDIFKFIDK KFKGSTEKYA
     QYVFEKSIVP YADKVKDFLN LPADKQKKIL DKDPAVALFN SVLPAIMQAQ DKSEEMMLNI
     EKGKREYFAA SRIMDPNRQM PSDANFTMRM SYGSIKGYAP KDGAWYNYYT TEQGVFEKQD
     PTSSEFAVQP EILSLLRSKD FGQYGVGDHL RLCFLSDNDI TGGNSGSPVF NGNGELIGLA
     FDGNWEAMSG DIEFEPDLQR TISVDIRYVL FMIDKWAKMP HLIKELNLVK GDQRDLMPAG
     KGGNCSHKKA QTCAKKECSK GKKCAEKSAT CISAMKDGKP CKTEKACAAG QKSAEKKANC
     CSTMKDGKPC TGDKDCAKSG KACCGKNKEA AAKKASKK