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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)DescriptionActionsGraphical viewLength
Active sitei603Charge relay systemBy similarity1
Active sitei678Charge relay systemBy similarity1
Active sitei710Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi205E → Q: Inactive. 1 Publication1
Mutagenesisi636E → A: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000039475725 – 732Prolyl tripeptidyl peptidaseSequence analysisAdd BLAST708
ChainiPRO_000039475881 – 732Prolyl tripeptidyl peptidase 75.8 kDa form1 PublicationAdd BLAST652

Post-translational modificationi

The N-terminus is blocked.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi242619.PG1361.

Structurei

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi58 – 60Combined sources3
Beta strandi63 – 68Combined sources6
Beta strandi71 – 75Combined sources5
Beta strandi85 – 88Combined sources4
Helixi89 – 93Combined sources5
Beta strandi111 – 115Combined sources5
Turni116 – 119Combined sources4
Beta strandi120 – 125Combined sources6
Beta strandi128 – 133Combined sources6
Turni134 – 137Combined sources4
Beta strandi138 – 143Combined sources6
Beta strandi158 – 165Combined sources8
Beta strandi168 – 173Combined sources6
Turni177 – 179Combined sources3
Beta strandi185 – 187Combined sources3
Beta strandi195 – 199Combined sources5
Helixi202 – 204Combined sources3
Beta strandi211 – 214Combined sources4
Beta strandi218 – 227Combined sources10
Beta strandi234 – 238Combined sources5
Beta strandi241 – 243Combined sources3
Beta strandi245 – 249Combined sources5
Beta strandi260 – 267Combined sources8
Turni268 – 271Combined sources4
Beta strandi272 – 275Combined sources4
Beta strandi285 – 291Combined sources7
Beta strandi295 – 303Combined sources9
Beta strandi309 – 316Combined sources8
Turni317 – 319Combined sources3
Beta strandi322 – 330Combined sources9
Beta strandi348 – 355Combined sources8
Beta strandi362 – 367Combined sources6
Beta strandi372 – 375Combined sources4
Beta strandi379 – 381Combined sources3
Beta strandi383 – 389Combined sources7
Beta strandi393 – 403Combined sources11
Beta strandi408 – 414Combined sources7
Beta strandi421 – 423Combined sources3
Beta strandi426 – 434Combined sources9
Beta strandi438 – 446Combined sources9
Beta strandi453 – 461Combined sources9
Beta strandi463 – 468Combined sources6
Beta strandi481 – 487Combined sources7
Beta strandi491 – 500Combined sources10
Beta strandi511 – 516Combined sources6
Helixi537 – 543Combined sources7
Beta strandi547 – 551Combined sources5
Beta strandi557 – 559Combined sources3
Helixi561 – 565Combined sources5
Turni566 – 569Combined sources4
Helixi573 – 587Combined sources15
Beta strandi592 – 602Combined sources11
Helixi604 – 615Combined sources12
Turni617 – 619Combined sources3
Beta strandi620 – 627Combined sources8
Helixi632 – 634Combined sources3
Helixi637 – 644Combined sources8
Turni647 – 649Combined sources3
Helixi651 – 657Combined sources7
Helixi659 – 665Combined sources7
Beta strandi668 – 675Combined sources8
Beta strandi679 – 681Combined sources3
Helixi684 – 696Combined sources13
Beta strandi701 – 705Combined sources5
Beta strandi709 – 711Combined sources3
Helixi716 – 731Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OMAiKGTFWSP.

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:PG_1361.
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
PDB 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.
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:PG_1361.
PATRICi22979764. VBIPorGin134034_1266.

Phylogenomic databases

eggNOGiENOG4105C5Z. Bacteria.
COG1506. LUCA.
KOiK18574.
OMAiKGTFWSP.

Enzyme and pathway databases

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...

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 2, 2016
This is version 76 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.