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C3L049 (PEPT_CLOB6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:CLJ_B0509
OrganismClostridium botulinum (strain 657 / Type Ba4) [Complete proteome] [HAMAP]
Taxonomic identifier515621 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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_1000211989

Sites

Active site801 By similarity
Active site1751Proton acceptor By similarity
Metal binding781Zinc 1 By similarity
Metal binding1411Zinc 1 By similarity
Metal binding1411Zinc 2 By similarity
Metal binding1761Zinc 2 By similarity
Metal binding1981Zinc 1 By similarity
Metal binding3801Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C3L049 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 2694F24CE04969AC

FASTA40845,624
        10         20         30         40         50         60 
MKDVLERFLG YIRIDTQSSE ESDTVPTTKT QLEFAKKLGE ELKAIGLKDV SVDENGYVMA 

        70         80         90        100        110        120 
TLESNIDKKV PTIGFIAHMD TSPDLSGTNI NPRIVEKYDG QDIVLNKEKN IVLKINEFPE 

       130        140        150        160        170        180 
ILEYKGQDIV VTDGNTLLGA DDKAGIAEII TAMEYLINHP EIKHGTIKVG FTPDEEVGKG 

       190        200        210        220        230        240 
ADHFDVKKFG ADLAYTLDGG GIGELECETF NAAKAKVIIE GRNVHPGSAK NKMTNAVLVA 

       250        260        270        280        290        300 
NKFINMLPEN EVPERTEGYE GFFHLLSVKS EVETAELNYI IRDFDRKKFE ERKEQIKEVG 

       310        320        330        340        350        360 
KKINEEYNKE IVCVKVEDQY YNMKEKIDEV KYVVDIAHDA MKAIDIEPIL VPIRGGTDGS 

       370        380        390        400 
RLSFMGLPTP NLFAGGHNFH GRFEFVPVLS MEKAAELVVK IAELYANR 

« Hide

References

[1]"Genome sequence of Clostridium botulinum Ba4 strain 657."
Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 657 / Type Ba4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001083 Genomic DNA. Translation: ACQ54839.1.
RefSeqYP_002861315.1. NC_012658.1.

3D structure databases

ProteinModelPortalC3L049.
SMRC3L049. Positions 1-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING515621.CLJ_B0509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ54839; ACQ54839; CLJ_B0509.
GeneID7880723.
KEGGcbi:CLJ_B0509.
PATRIC19409448. VBICloBot19908_0756.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2195.
HOGENOMHOG000032390.
KOK01258.
OMAHENYDGE.
OrthoDBEOG6SV59Q.

Enzyme and pathway databases

BioCycCBOT515621:GCP3-495-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_CLOB6
AccessionPrimary (citable) accession number: C3L049
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries