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B9EAD7 (PEPT_MACCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 35. 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:MCCL_0491
OrganismMacrococcus caseolyticus (strain JCSC5402) [Complete proteome] [HAMAP]
Taxonomic identifier458233 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Macrococcus ›

Protein attributes

Sequence length407 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 – 407407Peptidase T HAMAP-Rule MF_00550
PRO_1000200891

Sites

Active site801 By similarity
Active site1731Proton acceptor By similarity
Metal binding781Zinc 1 By similarity
Metal binding1391Zinc 1 By similarity
Metal binding1391Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding3781Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B9EAD7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 2383898DE69B7A8A

FASTA40745,438
        10         20         30         40         50         60 
MKEKLIDRLT SYVVIDTQSD ASSTTTPSTD KQWNLLNQLK QEIEQLGLET DIDEYGYLFA 

        70         80         90        100        110        120 
TLPSNTNKDV PVIGLLAHVD TATDFTGTNV NPQIIQSYDG NDITLKSGLK IETAKFPELS 

       130        140        150        160        170        180 
LYKGHTLITT DGTTLLGADN KAGIAEIMTA IEYLIAHPEI KHGKIRFGFT PDEEIGRGPH 

       190        200        210        220        230        240 
KFDVERFACD FAYTIDGGRR GELQYESFNA AGVNVTFNGV NVHPGSAKDK MVNALNLAVR 

       250        260        270        280        290        300 
FQSSLPANEV PEHTEGYEGF FHLMELNGNV ERAQLSYIIR DHSREQFEAR KVKMHEIITS 

       310        320        330        340        350        360 
IQNEYGEQAA HIEINDQYYN MGEKITPHPQ LIDIPLEVMK SLNIEPIVEP IRGGTDGSQL 

       370        380        390        400 
SYMGLPTPNL FTGGENYHGP YEYVSVDDME RAVMNIVGIL QKFEEKA

« Hide

References

[1]"Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC5402.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009484 Genomic DNA. Translation: BAH17198.1.
RefSeqYP_002559894.1. NC_011999.1.

3D structure databases

ProteinModelPortalB9EAD7.
ModBaseSearch...

Protein-protein interaction databases

STRING458233.MCCL_0491.

Protein family/group databases

MEROPSM20.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH17198; BAH17198; MCCL_0491.
GeneID7389604.
KEGGmcl:MCCL_0491.
PATRIC22423268. VBIMacCas48391_0577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMAYVYATIP.

Enzyme and pathway databases

BioCycMCAS458233:GI03-1763-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_MACCJ
AccessionPrimary (citable) accession number: B9EAD7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 1, 2013
This is version 35 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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