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Q2T0C0 (AMPA_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:
Probable cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase
Gene names
Name:pepA
Ordered Locus Names:BTH_I0823
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. HAMAP MF_00181

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP MF_00181

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP MF_00181

Subcellular location

Cytoplasm By similarity HAMAP MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: InterPro

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000019900

Sites

Active site2861 Potential
Active site3601 Potential
Metal binding2741Manganese 2 By similarity
Metal binding2791Manganese 1 By similarity
Metal binding2791Manganese 2 By similarity
Metal binding2971Manganese 2 By similarity
Metal binding3561Manganese 1 By similarity
Metal binding3581Manganese 1 By similarity
Metal binding3581Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T0C0 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5A16C203027195AB

FASTA50352,731
        10         20         30         40         50         60 
MDFSIKGCDW SKGSAKGFLT GKSDCIVLGV FEAQTLSGAA LDIDEAAKGL VSRVIKAGDI 

        70         80         90        100        110        120 
DGKLGKTLFL HEVSGIGASR VLLVGLGKQD AFSQKAYNDA VKAAWRALLG TKVVQVTFTL 

       130        140        150        160        170        180 
AQLPVPERAS DWGVRAAILA LRNETYKFTQ MKSKPDASAP ALKRIVFSVD PADEKAAKIA 

       190        200        210        220        230        240 
AKQAVALANG MDLTRDLGNL PGNVCTPTYL ANTAKKLAKD WGLKADVLGL KQIQALKMSS 

       250        260        270        280        290        300 
FLSVAKGSVE PPQFIVLHYQ GAAAKAAPVV LVGKGITFDS GGISLKPGEG MDEMKYDMCG 

       310        320        330        340        350        360 
AGSVLGTIRA VAEMGLKINV VAIVPTCENM PAGNANKPGD IVTSMKGLTI EVLNTDAEGR 

       370        380        390        400        410        420 
LILCDALTYA ERFKPAAVID VATLTGACII ALGHHNTGLF SKDDALAGEL LDASREAGDP 

       430        440        450        460        470        480 
AWRLPLDDEY QDQLKSNFAD LANIGGRPAG SVTAACFLSR FAENYPWAHL DIAGTAWKSG 

       490        500 
AAKGATGRPV PLLAQFLIDR AGA 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC36801.1.
RefSeqYP_441379.1. NC_007651.1.

3D structure databases

HSSPHSSP built from PDB template 2EWB based on UniProtKB P00727.
ProteinModelPortalQ2T0C0.
SMRQ2T0C0. Positions 20-502.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2T0C0.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3847449.
GenomeReviewsGene locus BTH_I0823 in contig CP000086_GR.
KEGGbte:BTH_I0823.
PATRIC19304452. VBIBurTha36512_3542.
TIGRBTH_I0823.

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHBG742580.
OMAKYDWAHL.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I0823-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
[Tree]
InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
KOK01255.
PANTHERPTHR11963:SF3. Peptidase_M17. 1 hit.
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPA_BURTA
AccessionPrimary (citable) accession number: Q2T0C0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 41 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