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B5BAE8 (PEPT_SALPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:SSPA1508
OrganismSalmonella paratyphi A (strain AKU_12601) [Complete proteome] [HAMAP]
Taxonomic identifier554290 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length409 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

   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 – 409409Peptidase T HAMAP-Rule MF_00550
PRO_1000129044

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
B5BAE8 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: E2C66902B8C698DB

FASTA40944,921
        10         20         30         40         50         60 
MDKLLERFLH YVSLDTQSKS GVRQVPSTEG QWKLLRLLKQ QLEEMGLVNI TLSEKGTLMA 

        70         80         90        100        110        120 
TLPANVEGDI PAIGFISHVD TSPDFSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL 

       130        140        150        160        170        180 
HQLLGQTLIT TDGKTLLGAD DKAGVAEIMT ALAVLKGNPI PHGEIKVAFT PDEEVGKGAK 

       190        200        210        220        230        240 
HFDVEEFGAQ WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR 

       250        260        270        280        290        300 
IHAEVPADEA PETTEGYEGF YHLASMKGTV DRAEMHYIIR DFDRKQFEAR KRKMMEIAKK 

       310        320        330        340        350        360 
VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCHITPEMK PIRGGTDGAQ 

       370        380        390        400 
LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAKRGQ 

« Hide

References

[1]"Pseudogene accumulation in the evolutionary histories of Salmonella enterica serovars Paratyphi A and Typhi."
Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., Mungall K., Dougan G., Parkhill J.
BMC Genomics 10:36-36(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AKU_12601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM200053 Genomic DNA. Translation: CAR59691.1.
RefSeqYP_002142347.1. NC_011147.1.

3D structure databases

ProteinModelPortalB5BAE8.
SMRB5BAE8. Positions 1-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING554290.SSPA1508.

Protein family/group databases

MEROPSM20.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR59691; CAR59691; SSPA1508.
PATRIC32342998. VBISalEnt134303_1733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
OMADCYIEVT.
OrthoDBEOG6SV59Q.

Enzyme and pathway databases

BioCycSENT554290:GJDA-1613-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_SALPK
AccessionPrimary (citable) accession number: B5BAE8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 42 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