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Protein

Prolyl tripeptidyl peptidase

Gene

ptpA

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Serine proteinase. Releases tripeptides from the free amino terminus of proteins. Has a requirement for Pro in the P1 position, but is inactivated by Pro in the P1' position.1 Publication

Catalytic activityi

Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.1 Publication

Enzyme regulationi

Strongly inhibited by diisopropyl fluorophosphate and Pefabloc. Weakly inhibited by 3,4-dichloroisocumarin. Not inhibited by phenylmethylsulfonyl fluoride, leupeptin, antipain or prolinal. Activated by iodoacetamide.1 Publication

pH dependencei

Optimum pH is 6-8.1 Publication

Temperature dependencei

Stable for at least 12 hours at 25 or 37 degrees Celsius (at pH 7.6).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei603 – 6031Charge relay systemBy similarity
Active sitei678 – 6781Charge relay systemBy similarity
Active sitei710 – 7101Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciPGIN242619:GHX8-1230-MONOMER.
BRENDAi3.4.14.12. 756.

Protein family/group databases

ESTHERiporgi-q7muw6. DPP4N_Peptidase_S9.
MEROPSiS09.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl tripeptidyl peptidase1 Publication (EC:3.4.14.12)
Short name:
PTP1 Publication
Alternative name(s):
Prolyl tripeptidyl peptidase 81.8 kDa form1 Publication
Prolyl tripeptidyl peptidase A1 Publication
Cleaved into the following chain:
Prolyl tripeptidyl peptidase 75.8 kDa form1 Publication
Gene namesi
Name:ptpA1 Publication
Ordered Locus Names:PG_1361
OrganismiPorphyromonas gingivalis (strain ATCC BAA-308 / W83)
Taxonomic identifieri242619 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
Proteomesi
  • UP000000588 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051E → Q: Inactive. 1 Publication
Mutagenesisi636 – 6361E → A: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 732708Prolyl tripeptidyl peptidaseSequence analysisPRO_0000394757Add
BLAST
Chaini81 – 732652Prolyl tripeptidyl peptidase 75.8 kDa form1 PublicationPRO_0000394758Add
BLAST

Post-translational modificationi

The N-terminus is blocked.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi242619.PG1361.

Structurei

Secondary structure

1
732
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603Combined sources
Beta strandi63 – 686Combined sources
Beta strandi71 – 755Combined sources
Beta strandi85 – 884Combined sources
Helixi89 – 935Combined sources
Beta strandi111 – 1155Combined sources
Turni116 – 1194Combined sources
Beta strandi120 – 1256Combined sources
Beta strandi128 – 1336Combined sources
Turni134 – 1374Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi168 – 1736Combined sources
Turni177 – 1793Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi195 – 1995Combined sources
Helixi202 – 2043Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi218 – 22710Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi260 – 2678Combined sources
Turni268 – 2714Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi285 – 2917Combined sources
Beta strandi295 – 3039Combined sources
Beta strandi309 – 3168Combined sources
Turni317 – 3193Combined sources
Beta strandi322 – 3309Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 3897Combined sources
Beta strandi393 – 40311Combined sources
Beta strandi408 – 4147Combined sources
Beta strandi421 – 4233Combined sources
Beta strandi426 – 4349Combined sources
Beta strandi438 – 4469Combined sources
Beta strandi453 – 4619Combined sources
Beta strandi463 – 4686Combined sources
Beta strandi481 – 4877Combined sources
Beta strandi491 – 50010Combined sources
Beta strandi511 – 5166Combined sources
Helixi537 – 5437Combined sources
Beta strandi547 – 5515Combined sources
Beta strandi557 – 5593Combined sources
Helixi561 – 5655Combined sources
Turni566 – 5694Combined sources
Helixi573 – 58715Combined sources
Beta strandi592 – 60211Combined sources
Helixi604 – 61512Combined sources
Turni617 – 6193Combined sources
Beta strandi620 – 6278Combined sources
Helixi632 – 6343Combined sources
Helixi637 – 6448Combined sources
Turni647 – 6493Combined sources
Helixi651 – 6577Combined sources
Helixi659 – 6657Combined sources
Beta strandi668 – 6758Combined sources
Beta strandi679 – 6813Combined sources
Helixi684 – 69613Combined sources
Beta strandi701 – 7055Combined sources
Beta strandi709 – 7113Combined sources
Helixi716 – 73116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5LX-ray2.10A39-732[»]
2DCMX-ray2.90A39-732[»]
2EEPX-ray2.20A39-732[»]
2Z3WX-ray2.00A39-732[»]
2Z3ZX-ray1.95A39-732[»]
ProteinModelPortaliQ7MUW6.
SMRiQ7MUW6. Positions 53-732.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7MUW6.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105C5Z. Bacteria.
COG1506. LUCA.
KOiK18574.
OMAiMYGERYM.
OrthoDBiEOG6TXQV1.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7MUW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTIFQQLF LSVCALTVAL PCSAQSPETS GKEFTLEQLM PGGKEFYNFY
60 70 80 90 100
PEYVVGLQWM GDNYVFIEGD DLVFNKANGK SAQTTRFSAA DLNALMPEGC
110 120 130 140 150
KFQTTDAFPS FRTLDAGRGL VVLFTQGGLV GFDMLARKVT YLFDTNEETA
160 170 180 190 200
SLDFSPVGDR VAYVRNHNLY IARGGKLGEG MSRAIAVTID GTETLVYGQA
210 220 230 240 250
VHQREFGIEK GTFWSPKGSC LAFYRMDQSM VKPTPIVDYH PLEAESKPLY
260 270 280 290 300
YPMAGTPSHH VTVGIYHLAT GKTVYLQTGE PKEKFLTNLS WSPDENILYV
310 320 330 340 350
AEVNRAQNEC KVNAYDAETG RFVRTLFVET DKHYVEPLHP LTFLPGSNNQ
360 370 380 390 400
FIWQSRRDGW NHLYLYDTTG RLIRQVTKGE WEVTNFAGFD PKGTRLYFES
410 420 430 440 450
TEASPLERHF YCIDIKGGKT KDLTPESGMH RTQLSPDGSA IIDIFQSPTV
460 470 480 490 500
PRKVTVTNIG KGSHTLLEAK NPDTGYAMPE IRTGTIMAAD GQTPLYYKLT
510 520 530 540 550
MPLHFDPAKK YPVIVYVYGG PHAQLVTKTW RSSVGGWDIY MAQKGYAVFT
560 570 580 590 600
VDSRGSANRG AAFEQVIHRR LGQTEMADQM CGVDFLKSQS WVDADRIGVH
610 620 630 640 650
GWSYGGFMTT NLMLTHGDVF KVGVAGGPVI DWNRYEIMYG ERYFDAPQEN
660 670 680 690 700
PEGYDAANLL KRAGDLKGRL MLIHGAIDPV VVWQHSLLFL DACVKARTYP
710 720 730
DYYVYPSHEH NVMGPDRVHL YETITRYFTD HL
Length:732
Mass (Da):82,266
Last modified:December 15, 2003 - v1
Checksum:iFE08469EB5562810
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015924 Genomic DNA. Translation: AAQ66425.1.
RefSeqiWP_005873421.1. NC_002950.2.

Genome annotation databases

EnsemblBacteriaiAAQ66425; AAQ66425; PG_1361.
GeneIDi2551645.
KEGGipgi:PG1361.
PATRICi22979764. VBIPorGin134034_1266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015924 Genomic DNA. Translation: AAQ66425.1.
RefSeqiWP_005873421.1. NC_002950.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5LX-ray2.10A39-732[»]
2DCMX-ray2.90A39-732[»]
2EEPX-ray2.20A39-732[»]
2Z3WX-ray2.00A39-732[»]
2Z3ZX-ray1.95A39-732[»]
ProteinModelPortaliQ7MUW6.
SMRiQ7MUW6. Positions 53-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi242619.PG1361.

Protein family/group databases

ESTHERiporgi-q7muw6. DPP4N_Peptidase_S9.
MEROPSiS09.017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ66425; AAQ66425; PG_1361.
GeneIDi2551645.
KEGGipgi:PG1361.
PATRICi22979764. VBIPorGin134034_1266.

Phylogenomic databases

eggNOGiENOG4105C5Z. Bacteria.
COG1506. LUCA.
KOiK18574.
OMAiMYGERYM.
OrthoDBiEOG6TXQV1.

Enzyme and pathway databases

BioCyciPGIN242619:GHX8-1230-MONOMER.
BRENDAi3.4.14.12. 756.

Miscellaneous databases

EvolutionaryTraceiQ7MUW6.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-308 / W83.
  2. "Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis."
    Banbula A., Mak P., Bugno M., Silberring J., Dubin A., Nelson D., Travis J., Potempa J.
    J. Biol. Chem. 274:9246-9252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 81-97; 113-126 AND 597-612, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, BLOCKAGE OF N-TERMINUS.
  3. "Crystal structure and mechanism of tripeptidyl activity of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis."
    Ito K., Nakajima Y., Xu Y., Yamada N., Onohara Y., Ito T., Matsubara F., Kabashima T., Nakayama K., Yoshimoto T.
    J. Mol. Biol. 362:228-240(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-732.
  4. "Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism."
    Xu Y., Nakajima Y., Ito K., Zheng H., Oyama H., Heiser U., Hoffmann T., Gartner U.T., Demuth H.U., Yoshimoto T.
    J. Mol. Biol. 375:708-719(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 39-732 IN COMPLEX WITH INHIBITOR, MUTAGENESIS OF GLU-205 AND GLU-636.

Entry informationi

Entry nameiPTP_PORGI
AccessioniPrimary (citable) accession number: Q7MUW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: December 15, 2003
Last modified: November 11, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.