DPP11_POREA
ID DPP11_POREA Reviewed; 717 AA.
AC F8WQK8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Asp/Glu-specific dipeptidyl-peptidase {ECO:0000303|PubMed:21896480};
DE EC=3.4.14.- {ECO:0000269|PubMed:21896480};
DE AltName: Full=Dipeptidyl-peptidase 11 {ECO:0000303|PubMed:21896480};
DE Short=DPP11 {ECO:0000303|PubMed:21896480};
DE Flags: Precursor;
GN Name=dpp11; Synonyms=PeDPP11 {ECO:0000312|EMBL:BAK57291.1};
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 22-30, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-652 AND
RP ARG-670.
RC STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370;
RX PubMed=21896480; DOI=10.1074/jbc.m111.278572;
RA Ohara-Nemoto Y., Shimoyama Y., Kimura S., Kon A., Haraga H., Ono T.,
RA Nemoto T.K.;
RT "Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas
RT gingivalis ensures utilization of proteinaceous energy sources.";
RL J. Biol. Chem. 286:38115-38127(2011).
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. Shows a strict specificity for acidic residues (Asp or
CC Glu) in the P1 position, and has a hydrophobic residue preference at
CC the P2 position. Is likely involved in amino acid metabolism and
CC bacterial growth/survival of asaccharolytic P.endodontalis, that
CC utilizes amino acids from extracellular proteinaceous nutrients as
CC energy and carbon sources. {ECO:0000269|PubMed:21896480}.
CC -!- ACTIVITY REGULATION: Enzyme activity is completely blocked by
CC diisopropyl-fluorophosphates, moderately by phenylmethylsulfonyl
CC fluoride (PMSF) and 4-(2-methyl)benzenesulfonyl fluoride, and slightly
CC by pepstatin in vitro. {ECO:0000269|PubMed:21896480}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21896480};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21896480}. Cell
CC surface {ECO:0000269|PubMed:21896480}. Note=Is observed in both cell-
CC associated and soluble extracellular forms.
CC {ECO:0000269|PubMed:21896480}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR EMBL; AB610284; BAK57291.1; -; Genomic_DNA.
DR PDB; 5JWG; X-ray; 2.20 A; A/B=22-717.
DR PDB; 5JWI; X-ray; 2.10 A; A/B=22-717.
DR PDB; 5JXK; X-ray; 2.85 A; A/B=22-717.
DR PDB; 5JXP; X-ray; 2.50 A; A=22-717.
DR PDB; 5JY0; X-ray; 2.60 A; A=22-717.
DR PDBsum; 5JWG; -.
DR PDBsum; 5JWI; -.
DR PDBsum; 5JXK; -.
DR PDBsum; 5JXP; -.
DR PDBsum; 5JY0; -.
DR AlphaFoldDB; F8WQK8; -.
DR SMR; F8WQK8; -.
DR STRING; 553175.POREN0001_1130; -.
DR MEROPS; S46.002; -.
DR eggNOG; COG3591; Bacteria.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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 3D-structure; Aminopeptidase; Direct protein sequencing; Hydrolase;
KW Protease; Secreted; Serine protease; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:21896480"
FT CHAIN 22..717
FT /note="Asp/Glu-specific dipeptidyl-peptidase"
FT /id="PRO_5003379706"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14"
FT ACT_SITE 652
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:V5YM14,
FT ECO:0000305|PubMed:21896480"
FT SITE 670
FT /note="Is essential for the Asp/Glu P1 specificity of
FT DPP11; involved in the recognition of the Asp/Glu residue
FT at the P1 position of substrate peptides"
FT /evidence="ECO:0000250|UniProtKB:B2RID1,
FT ECO:0000305|PubMed:21896480"
FT MUTAGEN 652
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21896480"
FT MUTAGEN 670
FT /note="R->D: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21896480"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 210..218
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 317..346
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 349..366
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5JXP"
FT HELIX 423..440
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 520..561
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:5JXP"
FT STRAND 575..581
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 598..604
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5JXP"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 663..670
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 672..678
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:5JWI"
FT STRAND 688..692
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 693..701
FT /evidence="ECO:0007829|PDB:5JWI"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:5JWI"
FT HELIX 707..713
FT /evidence="ECO:0007829|PDB:5JWI"
SQ SEQUENCE 717 AA; 81096 MW; 4F99877BCCCABF3B CRC64;
MNKRFFPTLL LAFVCSTLAY ADGGMWLMQQ INGQVARMKS LGMQLEAADI YNPNGSSLKD
AVVMFDGGCT GVLVSNQGLL LTNHHCGYDQ IQKHSSVQHN YLKDGFWSYS LAEELVNPGL
EVEIVDEITD VTAAVKKELE RIKKPSGLEF LSPRYLSSLA PEIVGKKAAS RPGYRYEIKA
FYGGNRYYMF TKKVFRDVRL VAAPPSSIGK FGSDTDNWAW PRHTGDFSIF RLYADKNGNP
AEYSKDNVPY RPKRWVKVNA QGVKEGDFAL IMGYPGTTYK FFTADEVTEW SEIDNNIRIE
MRGILQDVML REMLADPKIN IMYAAKYASS QNGYKRAQGA NWAIRRRSLR EIKLAQQQEV
LAWAKQKGIA TTEEAVRAIS KAIEGRQDLR MRQRYLLEGI LMGIEMSNAP AADSDIADHW
DDPARREAGL QSIRKQFEAF FNKDYSPEVE KDQLAIALLT RYAERIPAEK QPISIREGIA
EYGSAKAYVE MIFDKSIYAS RERFEEFMKN PDRDRLLRDP MSRFAASVAY EHQKLAKEVA
AFDAPLAAAQ RSYVASVLDM KGQPNLAPDA NLTLRFTYGE IKGYQPRDVV TYGAKSTLEG
VMEKEDPNNW EYVVDPKLKA LYEAKNYGRY ANSDGSMPVN FCATTHTTGG NSGSPVMNAR
GELIGLNFDR NWEGVGGDIE YLPNYQRSII LDIRYLLFII DKFAGCQRLI DEIQPQF
