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P65805 (PEPT_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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:SAV0743
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 408408Peptidase T HAMAP-Rule MF_00550
PRO_0000185316

Sites

Active site801 By similarity
Active site1741Proton acceptor By similarity
Metal binding781Zinc 1 By similarity
Metal binding1401Zinc 1 By similarity
Metal binding1401Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding1971Zinc 1 By similarity
Metal binding3791Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P65805 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 28A88DC436056671

FASTA40845,820
        10         20         30         40         50         60 
MKNQLIDRLT RYTTIDTQSD PKSTTTPSTE KQWDLLHLLE KELQQLGLPT DLDENGYLFA 

        70         80         90        100        110        120 
TLESNIDADV PTVGFLAHVD TSPDFNASNV KPQIIENYDG KPYKLGNTKR VLDPKVFPEL 

       130        140        150        160        170        180 
NSLVGHTLMV TDGTSLLGAD DKAGIVEIME AICYLQEHPE IKHGTIRIGF TPDEEIGRGP 

       190        200        210        220        230        240 
HKFDVDRFNA DFAYTMDGSQ YGELQYESFN AAEAVITCHG VNVHPGSAKN AMVNAIRLGE 

       250        260        270        280        290        300 
QFDSLLPDSE VPERTEGYEG FYHLMNFEGT VEKATLQYII RDHDKKQFEL RKKRILEIRD 

       310        320        330        340        350        360 
DINAHFENYP VKVDISDQYF NMAEKILPLP HIIDIPKRVF AKLDIPANTE PIRGGTDGSQ 

       370        380        390        400 
LSFMGLPTPN IFTGCGNFHG PYEYASIDVM EKAVQVIIGI VEDIAENH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB56905.1.
RefSeqNP_371267.1. NC_002758.2.

3D structure databases

ProteinModelPortalP65805.
SMRP65805. Positions 1-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158878.SAV0743.

2D gel databases

World-2DPAGE0002:P65805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB56905; BAB56905; SAV0743.
GeneID1120716.
KEGGsav:SAV0743.
PATRIC19562158. VBIStaAur52173_0760.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMADCYIEVT.
OrthoDBEOG6SV59Q.
PhylomeDBP65805.

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-760-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_STAAM
AccessionPrimary (citable) accession number: P65805
Secondary accession number(s): Q99VN1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 69 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