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Q2YSI6 (PEPT_STAAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SAB0695c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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.

Subcellular location

Cytoplasm By similarity.

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: 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: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Peptidase T HAMAP-Rule MF_00550
PRO_0000274021

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
Q2YSI6 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 16B7207F9C35184C

FASTA40845,855
        10         20         30         40         50         60 
MKNQLIDRLT RYTTIDTQSD PKSTTTPSTE KQWDLLHLLE RELQQLGLPT DLDENGYLFA 

        70         80         90        100        110        120 
TLESNIDADV PTVGFLAHVD TSPDFNASNV KPQIIENYDS 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 VEDIAENN

« Hide

References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ938182 Genomic DNA. Translation: CAI80383.1.
RefSeqYP_416188.1. NC_007622.1.

3D structure databases

ProteinModelPortalQ2YSI6.
ModBaseSearch...

Protein-protein interaction databases

STRING273036.SAB0695c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI80383; CAI80383; SAB0695c.
GeneID3794463.
KEGGsab:SAB0695c.
PATRIC19522185. VBIStaAur92441_0744.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMAYVYATIP.
ProtClustDBPRK05469.

Enzyme and pathway databases

BioCycSAUR273036:GJVS-714-MONOMER.

Family and domain databases

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. Peptidase_M20_dimer. 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_STAAB
AccessionPrimary (citable) accession number: Q2YSI6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 20, 2005
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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