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P42778 (AMPT_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase T
Short name=AP-T
EC=3.4.11.-
Alternative name(s):
Heat-stable aminopeptidase
Gene names
Ordered Locus Names:TTHA1152
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

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

General annotation (Comments)

Function

Metal-dependent exopeptidase. Ref.3

Cofactor

Binds 2 divalent metal cations per subunit. Can use cobalt, zinc, and possibly also magnesium ions. Ref.3

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the peptidase M29 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Aminopeptidase T
PRO_0000079176

Sites

Metal binding2501Divalent metal cation 1
Metal binding3161Divalent metal cation 1
Metal binding3161Divalent metal cation 2
Metal binding3401Divalent metal cation 1
Metal binding3401Divalent metal cation 2
Metal binding3451Divalent metal cation 1
Metal binding3761Divalent metal cation 2
Metal binding3781Divalent metal cation 2

Secondary structure

1 ......................................................................... 408
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42778 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CBA7F8E0DA99A2D2

FASTA40845,018
        10         20         30         40         50         60 
MDAFKRNLEK LAELAIRVGL NLEKGQEVIA TAPIEAVDFV RLLAEKAYRE GASLFTVIYG 

        70         80         90        100        110        120 
DQELARKRLA LAPEEGLDKA PAWLYEGMAR AFREGAARLA VSGSDPKALE GLPPEKVGRA 

       130        140        150        160        170        180 
QKANARAYKP ALEAITEFVT NWTIVPFAHP GWARAVFPGL PEEEAVRRLW EAIFQATRAD 

       190        200        210        220        230        240 
QEDPIAAWEA HNRALHEKVA YLNARRFHAL HFKGPGTDLV VGLAEGHLWQ GGATATKGGR 

       250        260        270        280        290        300 
LCNPNLPTEE VFTAPHRERV EGVVRASRPL ALGGTLVEGI FARFERGFAV EVRAEKGEEV 

       310        320        330        340        350        360 
LRRLLDTDEG ARRLGEVALV PADNPIAKTG LVFFDTLFDE NAASHIAFGQ AYQENLEGRP 

       370        380        390        400 
SGEAFRKRGG NESLVHVDWM IGSEEMDVDG LYEDGTRTPL MRRGRWVV

« Hide

References

« Hide 'large scale' references
[1]"Cloning of genes of the aminopeptidase T family from Thermus thermophilus HB8 and Bacillus stearothermophilus NCIB8924: apparent similarity to the leucyl aminopeptidase family."
Motoshima H., Minagawa E., Tsukasaki F., Kaminogawa S.
Biosci. Biotechnol. Biochem. 61:1710-1717(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Substrate access to the active sites in aminopeptidase T, a representative of a new metallopeptidase clan."
Odintsov S.G., Sabala I., Bourenkov G., Rybin V., Bochtler M.
J. Mol. Biol. 354:403-412(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13386 Genomic DNA. Translation: BAA02654.1.
AP008226 Genomic DNA. Translation: BAD70975.1.
RefSeqYP_144418.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYIX-ray3.70A/B/C/D/E1-408[»]
ProteinModelPortalP42778.
SMRP42778. Positions 3-408.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA1152.

Protein family/group databases

MEROPSM29.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70975; BAD70975; BAD70975.
GeneID3170035.
KEGGttj:TTHA1152.
PATRIC23957265. VBITheThe93045_1132.

Phylogenomic databases

eggNOGCOG2309.
HOGENOMHOG000023469.
KOK01269.
OMAHIALGRC.
ProtClustDBCLSK864714.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1184-MONOMER.

Family and domain databases

InterProIPR000787. Peptidase_M29.
[Graphical view]
PfamPF02073. Peptidase_M29. 1 hit.
[Graphical view]
PRINTSPR00919. THERMOPTASE.
ProtoNetSearch...

Other

EvolutionaryTraceP42778.

Entry information

Entry nameAMPT_THET8
AccessionPrimary (citable) accession number: P42778
Secondary accession number(s): Q5SJ62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 29, 2013
This is version 64 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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