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A4TLP0 (PEPT_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidase T

EC=3.4.11.4
Alternative name(s):
Aminotripeptidase
Short name=Tripeptidase
Tripeptide aminopeptidase
Gene names
Name:pepT
Ordered Locus Names:YPDSF_1817
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves the N-terminal amino acid of tripeptides By similarity. HAMAP-Rule MF_00550

Catalytic activity

Release of the N-terminal residue from a tripeptide. HAMAP-Rule MF_00550

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00550

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00550.

Sequence similarities

Belongs to the peptidase M20B family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpeptide metabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

tripeptide aminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Peptidase T HAMAP-Rule MF_00550
PRO_1000017857

Sites

Active site801 By similarity
Active site1731Proton acceptor By similarity
Metal binding781Zinc 1 By similarity
Metal binding1401Zinc 1 By similarity
Metal binding1401Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding3791Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TLP0 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 2D6E4D50923FC555

FASTA41145,387
        10         20         30         40         50         60 
MDKLLDRFFN YVSFDTQAKA NVKSVPSTQG QRKLAQALQQ ELLTLGFSHV TLSDHGCVMA 

        70         80         90        100        110        120 
TLPANVSWPV PTIGFIAHLD TSPDFSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL 

       130        140        150        160        170        180 
HQLLGHTLIT TDGKTLLGAD DKAGIAEIIT AMVRLKHRNV PHGDIRIAFT PDEEVGKGAQ 

       190        200        210        220        230        240 
FFNVAEFDAQ WAYTVDGGGI GELEFENFNA ASVAIKIVGN NVHPGSAKGV MVNALSLATR 

       250        260        270        280        290        300 
YHQELPVDET PECTEGYDGF YHLQSIKGTV ERAEMHYIVR DFNRDSFEAR KKNMVDIAKR 

       310        320        330        340        350        360 
VGKGLHRDCY IEIVIDDSYY NMREQIIKHP HIIELAQQAM LDCDITPIMK PIRGGTDGAQ 

       370        380        390        400        410 
LSFKGLPCPN IFTGGYNYHG KHEFITLEGM EKAVAVIMRI SELTAKRAKE S 

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000668 Genomic DNA. Translation: ABP40202.1.
RefSeqYP_001163175.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TLP0.
SMRA4TLP0. Positions 1-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386656.YPDSF_1817.

Protein family/group databases

MEROPSM20.003.

Proteomic databases

PRIDEA4TLP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP40202; ABP40202; YPDSF_1817.
GeneID5064268.
KEGGypp:YPDSF_1817.
PATRIC18612966. VBIYerPes122972_2385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMAYVYATIP.
OrthoDBEOG6SV59Q.
ProtClustDBPRK05469.

Enzyme and pathway databases

BioCycYPES386656:GKD7-1853-MONOMER.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
HAMAPMF_00550. Aminopeptidase_M20.
InterProIPR001261. ArgE/DapE_CS.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
IPR010161. Peptidase_M20B.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF037215. Peptidase_M20B. 1 hit.
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01882. peptidase-T. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEPT_YERPP
AccessionPrimary (citable) accession number: A4TLP0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries