DPP5_PORG3
ID DPP5_PORG3 Reviewed; 684 AA.
AC B2RIT0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Dipeptidyl-peptidase 5 {ECO:0000303|PubMed:24398682};
DE Short=DPP5 {ECO:0000303|PubMed:24398682};
DE EC=3.4.14.- {ECO:0000269|PubMed:24398682};
DE AltName: Full=MER034615 {ECO:0000303|PubMed:24398682};
DE Flags: Precursor;
GN Name=dpp5 {ECO:0000303|PubMed:24398682};
GN OrderedLocusNames=PGN_0756 {ECO:0000312|EMBL:BAG33275.1};
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 25-35, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT,
RP AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=24398682; DOI=10.1074/jbc.m113.527333;
RA Ohara-Nemoto Y., Rouf S.M., Naito M., Yanase A., Tetsuo F., Ono T.,
RA Kobayakawa T., Shimoyama Y., Kimura S., Nakayama K., Saiki K., Konishi K.,
RA Nemoto T.K.;
RT "Identification and characterization of prokaryotic dipeptidyl-peptidase 5
RT from Porphyromonas gingivalis.";
RL J. Biol. Chem. 289:5436-5448(2014).
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. Prefers Ala and hydrophobic residues except Pro at the
CC P1 position, and has no preference for P2 residues. Shows high
CC dipeptidyl peptidase activity toward the synthetic substrates Lys-Ala-,
CC Gly-Phe-, Met-Leu-, and Ser-Tyr-methylcoumaryl-7-amide (MCA), and
CC slowly hydrolyzes Val-Tyr-MCA. 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. {ECO:0000269|PubMed:24398682}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=396 uM for Gly-Phe-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=688 uM for Lys-Ala-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=701 uM for Met-Leu-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=151 uM for Lys-Phe-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=296 uM for Ser-Tyr-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=146 uM for Lys-Leu-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC KM=220 uM for Lys-Val-MCA (at 37 degrees Celsius and pH 6.0)
CC {ECO:0000269|PubMed:24398682};
CC Note=kcat is 5638 sec(-1) with Gly-Phe-MCA as substrate. kcat is 7577
CC sec(-1) with Lys-Ala-MCA as substrate. kcat is 5562 sec(-1) with Met-
CC Leu-MCA as substrate. kcat is 744 sec(-1) with Lys-Phe-MCA as
CC substrate. kcat is 1329 sec(-1) with Ser-Tyr-MCA as substrate. kcat
CC is 490 sec(-1) with Lys-Leu-MCA as substrate. kcat is 299 sec(-1)
CC with Lys-Val-MCA as substrate (at 37 degrees Celsius and pH 6.0).
CC {ECO:0000269|PubMed:24398682};
CC pH dependence:
CC Optimum pH is 6.7, using Lys-Ala-MCA as substrate.
CC {ECO:0000269|PubMed:24398682};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24398682}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:24398682}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family.
CC {ECO:0000305|PubMed:24398682}.
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DR EMBL; AP009380; BAG33275.1; -; Genomic_DNA.
DR RefSeq; WP_012457755.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RIT0; -.
DR SMR; B2RIT0; -.
DR STRING; 431947.PGN_0756; -.
DR MEROPS; S09.075; -.
DR PRIDE; B2RIT0; -.
DR EnsemblBacteria; BAG33275; BAG33275; PGN_0756.
DR GeneID; 29255975; -.
DR KEGG; pgn:PGN_0756; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_008615_0_2_10; -.
DR OMA; YKHWDEW; -.
DR BioCyc; PGIN431947:G1G2V-828-MON; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
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:0042803; F:protein homodimerization activity; 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; 2.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Periplasm; Protease;
KW Repeat; Serine protease; Signal; WD repeat.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:24398682"
FT CHAIN 25..684
FT /note="Dipeptidyl-peptidase 5"
FT /id="PRO_5002781709"
FT REPEAT 87..127
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 220..259
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 323..363
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT ACT_SITE 542
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24398682"
FT ACT_SITE 627
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24398682"
FT ACT_SITE 659
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24398682"
SQ SEQUENCE 684 AA; 77455 MW; A6B8D87CD2479B56 CRC64;
MNKKIFSMMA ASIIGSAAMT PSAGTNTGEH LTPELFMTLS RVSEMALSPD GKTAVYAVSF
PDVKTNKATR ELFTVNLDGS GRKQITDTES NEYAPAWMAD GKRIAFMSNE GGSMQLWVMN
ADGTERRQLS NIEGGITGFL FSPDEKQVLF TKDIKFGKRT KDIYPDLDKA TGRIITDLMY
KHWDEWVETI PHPFIANATD GMITTGKDIM EGEPYEAPMK PWSGIEDFSW SPDGQNIAYA
SRKKTGMAYS LSTNSDIYIY NLTSGRTHNI SEGMMGYDTY PKFSPDGKSI AWISMERDGY
ESDLKRLFVA DLATGKRTHV NPTFDYNVDM IQWAPDSKGI YFLACKEAET NLWEITLKTG
KIRQITQGQH DYADFSVRND VMLAKRHSFE LPDDLYRVNP KNGAAQAVTA ENKAILDRLT
PIACEKRWMK TTDGGNMLTW VVLPPDFDKN KKYPAILYCQ GGPQNTVSQF WSFRWNLRLM
AEQGYIVIAP NRHGVPGFGQ KWNEQISGDY GGQNMRDYLT AVDEMKKEPY VDGDRIGAVG
ASYGGFSVYW LAGHHDKRFA AFIAHAGIFN LEMQYATTEE MWFANWDIGG PFWEKDNVVA
QRTYATSPHK YVQNWDTPIL MIHGELDFRI LASQAMAAFD AAQLRGVPSE MLIYPDENHW
VLQPQNALLF HRTFFGWLDR WLKK
