DPP5_POREA
ID DPP5_POREA Reviewed; 691 AA.
AC C3J8X2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Dipeptidyl-peptidase 5 {ECO:0000303|PubMed:25494328};
DE Short=DPP5 {ECO:0000303|PubMed:25494328};
DE EC=3.4.14.- {ECO:0000269|PubMed:25494328};
DE AltName: Full=MER236725 {ECO:0000303|PubMed:25494328};
DE Flags: Precursor;
GN Name=dpp5 {ECO:0000303|PubMed:25494328};
GN ORFNames=POREN0001_0643 {ECO:0000312|EMBL:EEN83452.1};
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, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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. Prefers Ala and hydrophobic residues at the P1 position,
CC and has no preference for P2 residues. Shows the highest dipeptidyl
CC peptidase activity toward the synthetic substrate Lys-Ala-
CC methylcoumaryl-7-amide (Lys-Ala-MCA). Is likely involved in amino acid
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for Lys-Ala-MCA (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:25494328};
CC KM=196 uM for Met-Leu-MCA (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:25494328};
CC KM=257 uM for Ser-Tyr-MCA (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:25494328};
CC KM=993 uM for Gly-Phe-MCA (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:25494328};
CC Note=kcat is 21213 sec(-1) with Lys-Ala-MCA as substrate. kcat is
CC 5175 sec(-1) with Met-Leu-MCA as substrate. kcat is 3468 sec(-1) with
CC Ser-Tyr-MCA as substrate. kcat is 10378 sec(-1) with Gly-Phe-MCA as
CC substrate. {ECO:0000269|PubMed:25494328};
CC pH dependence:
CC Optimum pH is 6.7, using Lys-Ala-MCA as substrate.
CC {ECO:0000269|PubMed:25494328};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B2RIT0}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:B2RIT0}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; ACNN01000007; EEN83452.1; -; Genomic_DNA.
DR AlphaFoldDB; C3J8X2; -.
DR SMR; C3J8X2; -.
DR STRING; 553175.POREN0001_0643; -.
DR MEROPS; S09.075; -.
DR EnsemblBacteria; EEN83452; EEN83452; POREN0001_0643.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR OMA; YKHWDEW; -.
DR Proteomes; UP000004295; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Periplasm; Protease; Reference proteome;
KW Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..691
FT /note="Dipeptidyl-peptidase 5"
FT /id="PRO_5002927988"
FT ACT_SITE 549
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:B2RIT0"
FT ACT_SITE 634
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:B2RIT0"
FT ACT_SITE 666
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:B2RIT0"
SQ SEQUENCE 691 AA; 78098 MW; 27DC8F8FCEFAED84 CRC64;
MKRTILSLLA AVSLAIPVYA AGYSDGNPTQ QTSQSSMMTP EMLLTMARIG GFSLSPNGKQ
VVYSVSLPSI QDNKAKTQLF FVNSDGSGRK ALTDGTRTAV SPRWIEDGKR IAYLTVIEGE
MQLVSILPDG TDQRQVTRIP GGITGYLYSQ DGKQLVYTAD IKLPNEAKDR NPDLDKISGR
VITDLMYKHW DEWVETAPHT FVASLAQQPI TQGKDLLEGE LFEAPMKPHS DESDIAITPD
GKGIAYASRK KTGLEYSIST NSDIYYYDLT TGTTTNLTEG MMGYDTHPSF SPDGKYMTWC
SMERDGYESD LIRLFLLDRT TGEKTYLTEG FEYNVEQPTW SQDGKSIYFI ACVEAESHLY
ELTLKNKKIR RITQGQMDYV GFDLQGTTLV AARQSMLAPT DLYRIDLKKG TATAITKENE
STLAQLGDIR CEKRWMNTTN GEKMLVWVLY PANFDASKKY PSILYCQGGP QSTISQFWSY
RWNPRIMAEN GYIVILPNRH GVPGFGKAWN EQISGDYGGQ NMRDYLTAAD EMKKESYIDP
NGMGCVGASY GGFSVYWLAG HHEKRFNCFI AHAGIFNLEA QYLETEEKWF ANWDMGGAPW
EKSNATAQRT FATSPHLFVD KWDTPILIIH GERDYRILAS QGMMAFDAAR MHGVPTEMLL
YPDENHWVLQ PQNAVLWQRT FFRWLDRWLK K
