DPP7_PORG3
ID DPP7_PORG3 Reviewed; 712 AA.
AC B2RKV3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Dipeptidyl-peptidase 7 {ECO:0000303|PubMed:11096098};
DE Short=DPP-7 {ECO:0000303|PubMed:11096098};
DE Short=DPP7;
DE EC=3.4.14.- {ECO:0000269|PubMed:11096098};
DE Flags: Precursor;
GN Name=dpp7 {ECO:0000312|EMBL:BAG33998.1};
GN Synonyms=dpp-7 {ECO:0000303|PubMed:11096098};
GN OrderedLocusNames=PGN_1479 {ECO:0000312|EMBL:BAG33998.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
RN [2]
RP PROTEIN SEQUENCE OF 24-48; 245-250; 392-396; 409-414; 445-450; 489-493 AND
RP 549-554, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=HG66;
RX PubMed=11096098; DOI=10.1074/jbc.m008789200;
RA Banbula A., Yen J., Oleksy A., Mak P., Bugno M., Travis J., Potempa J.;
RT "Porphyromonas gingivalis DPP-7 represents a novel type of
RT dipeptidylpeptidase.";
RL J. Biol. Chem. 276:6299-6305(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-666.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
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 (PubMed:11096098, PubMed:23246913). Shows a broad
CC specificity for both aliphatic and aromatic residues in the P1
CC position, with glycine or proline being not acceptable in this position
CC (PubMed:11096098). Most potently cleaves the synthetic substrate Met-
CC Leu-methylcoumaryl-7-amide (Met-Leu-MCA), Leu-Arg-MCA and Lys-Ala-MCA
CC to a lesser extent (PubMed:23246913). Is likely involved in amino acid
CC metabolism and bacterial growth of asaccharolytic P.gingivalis, that
CC utilizes amino acids from extracellular proteinaceous nutrients as
CC energy and carbon sources (PubMed:11096098).
CC {ECO:0000269|PubMed:11096098, ECO:0000269|PubMed:23246913}.
CC -!- ACTIVITY REGULATION: Is inhibited in vitro by typical serine protease
CC inhibitors like diisopropyl fluorophosphate, Pefablock, and 3,4-
CC dichloroisocoumarin, but not by typical cysteine class inhibitors such
CC as E-64 or iododoacetic acid. {ECO:0000269|PubMed:11096098}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=313 uM for Ala-Ala-pNA {ECO:0000269|PubMed:11096098};
CC KM=441 uM for Ala-Phe-pNA {ECO:0000269|PubMed:11096098};
CC KM=256 uM for Gly-Ala-pNA {ECO:0000269|PubMed:11096098};
CC pH dependence:
CC Is active against Ala-Phe-pNA over a broad pH range, from neutral to
CC basic pH (6.5-9.0). {ECO:0000269|PubMed:11096098};
CC Temperature dependence:
CC Optimum temperature is 43 degrees Celsius, using Ala-Phe-pNA as
CC substrate. {ECO:0000269|PubMed:11096098};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:11096098}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR EMBL; AP009380; BAG33998.1; -; Genomic_DNA.
DR AlphaFoldDB; B2RKV3; -.
DR SMR; B2RKV3; -.
DR STRING; 431947.PGN_1479; -.
DR MEROPS; S46.001; -.
DR PRIDE; B2RKV3; -.
DR EnsemblBacteria; BAG33998; BAG33998; PGN_1479.
DR KEGG; pgn:PGN_1479; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OMA; KDWFFNP; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
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; Cell outer membrane; Coiled coil;
KW Direct protein sequencing; Hydrolase; Membrane; Protease; Serine protease;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11096098"
FT CHAIN 24..712
FT /note="Dipeptidyl-peptidase 7"
FT /id="PRO_5002780320"
FT COILED 136..173
FT /evidence="ECO:0000255"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 648
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT SITE 666
FT /note="Critical for substrate specificity of DPP7"
FT /evidence="ECO:0000269|PubMed:23246913"
FT MUTAGEN 666
FT /note="G->A: 61% of wild-type catalytic activity toward
FT Met-Leu-MCA."
FT /evidence="ECO:0000269|PubMed:23246913"
FT MUTAGEN 666
FT /note="G->D: Nearly abolishes catalytic activity toward
FT Met-Leu-MCA."
FT /evidence="ECO:0000269|PubMed:23246913"
FT MUTAGEN 666
FT /note="G->R: 22% of wild-type catalytic activity toward
FT Met-Leu-MCA. Acquires activity toward Leu-Asp- and Leu-Glu-
FT MCA."
FT /evidence="ECO:0000269|PubMed:23246913"
SQ SEQUENCE 712 AA; 80107 MW; F2D9037122993158 CRC64;
MQMKLKSILL GAALLLGASG VAKADKGMWL LNELNQENLD RMRELGFTLP LDSLYSFDKP
SIANAVVIFG GGCTGITVSD QGLIFTNHHC GYGAIQSQST VDHDYLRDGF VSRTMGEELP
IPGLSVKYLR KIVKVTDKVE GQLKGITDEM ERLRKAQEVC QELAKKENAD ENQLCIVEPF
YSNNEYFLIV YDVFKDVRMV FAPPSSVGKF GGDTDNWMWP RHTGDFSVFR VYAGADNRPA
EYSKDNKPYK PVYFAAVSMQ GYKADDYAMT IGFPGSTDRY LTSWGVEDRI ENENNPRIEV
RGIKQGIWKE AMSADQATRI KYASKYAQSA NYWKNSIGMN RGLARLDVIG RKRAEERAFA
DWIRKNGKSA VYGDVLSSLE KAYKEGAKAN REMTYLSETL FGGTEVVRFA QFANALATNP
DAHAGILKSL DDKYKDYLPS LDRKVLPAML DIVRRRIPAD KLPDIFKNVI DKKFKGDTKK
YADFVFDKSV VPYSDKFHAM LKSMDKEKFA KAIEKDPAVE LSKSVIAAAR AIQADAMANA
YAIEKGKRLF FAGLREMYPG RALPSDANFT MRMSYGSIKG YEPQDGAWYN YHTTGKGVLE
KQDPKSDEFA VQENILDLFR TKNYGRYAEN GQLHIAFLSN NDITGGNSGS PVFDKNGRLI
GLAFDGNWEA MSGDIEFEPD LQRTISVDIR YVLFMIDKWG QCPRLIQELK LI
