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A6TZM2 (PEPT_STAA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:SaurJH1_0784
OrganismStaphylococcus aureus (strain JH1) [Complete proteome] [HAMAP]
Taxonomic identifier359787 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length408 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 – 408408Peptidase T HAMAP-Rule MF_00550
PRO_1000081962

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
A6TZM2 [UniParc].

Last modified August 21, 2007. 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

References

[1]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH1."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000736 Genomic DNA. Translation: ABR51640.1.
RefSeqYP_001315927.1. NC_009632.1.

3D structure databases

ProteinModelPortalA6TZM2.
SMRA6TZM2. Positions 1-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359787.SaurJH1_0784.

Protein family/group databases

MEROPSM20.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR51640; ABR51640; SaurJH1_0784.
GeneID5315776.
KEGGsah:SaurJH1_0784.
PATRIC19533415. VBIStaAur98826_0820.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMADCYIEVT.
OrthoDBEOG6SV59Q.

Enzyme and pathway databases

BioCycSAUR359787:GCG4-805-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_STAA2
AccessionPrimary (citable) accession number: A6TZM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 52 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