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A9AJ16 (LFTR_BURM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Leucyl/phenylalanyl-tRNA--protein transferase

EC=2.3.2.6
Alternative name(s):
L/F-transferase
Leucyltransferase
Phenyalanyltransferase
Gene names
Name:aat
Ordered Locus Names:Bmul_1676, BMULJ_01567
OrganismBurkholderia multivorans (strain ATCC 17616 / 249) [Complete proteome] [HAMAP]
Taxonomic identifier395019 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine By similarity. HAMAP-Rule MF_00688

Catalytic activity

L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + L-leucyl-[protein]. HAMAP-Rule MF_00688

L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein]. HAMAP-Rule MF_00688

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00688.

Sequence similarities

Belongs to the L/F-transferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionleucyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_1000131909

Sequences

Sequence LengthMass (Da)Tools
A9AJ16 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 0D3160C18E69D1A2

FASTA25428,073
        10         20         30         40         50         60 
MVPWLGPDDP FPPVERALGP ATGAPGLLAA SADLLPSRLI DAYLRGIFPW YSDGQPVLWW 

        70         80         90        100        110        120 
SPDPRMILVP DEFKVSPSLK KTLKRVLRDP AWEVRVDHDF RGVMRACAQA PRRGQRGTWI 

       130        140        150        160        170        180 
TAEIIDAYSS LYRSGNAHSI ETWHDGRRVG GLYGVAFGQM FFGESMYADV TDASKIALAA 

       190        200        210        220        230        240 
LVAHLREHGL EMIDCQQNTS HLASLGGREI ARKAFVAHVR RAVAEPPIPW QFDKRVLAAL 

       250 
TGRTEPAAPS GIER 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.
[2]"Complete genome sequence of Burkholderia multivorans ATCC 17616."
Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000868 Genomic DNA. Translation: ABX15364.1.
AP009385 Genomic DNA. Translation: BAG43493.1.
RefSeqYP_001579861.1. NC_010084.1.
YP_001946029.1. NC_010804.1.

3D structure databases

ProteinModelPortalA9AJ16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395019.Bmul_1676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX15364; ABX15364; Bmul_1676.
BAG43493; BAG43493; BMULJ_01567.
GeneID5766931.
6358997.
KEGGbmj:BMULJ_01567.
bmu:Bmul_1676.
PATRIC19164908. VBIBurMul203716_2532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2360.
HOGENOMHOG000102325.
KOK00684.
OMAWSPDPRG.
OrthoDBEOG6WX4R3.

Enzyme and pathway databases

BioCycBMUL395019:GIYO-1566-MONOMER.

Family and domain databases

HAMAPMF_00688. Leu_Phe_trans.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR00667. aat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLFTR_BURM1
AccessionPrimary (citable) accession number: A9AJ16
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 47 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