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P0A8P1 (LFTR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:ycaA
Ordered Locus Names:b0885, JW0868
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00688.

Sequence similarities

Belongs to the L/F-transferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process via the N-end rule pathway

Inferred by curator PubMed 1962196. Source: EcoliWiki

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 4909560. Source: EcoliWiki

   Molecular_functionleucyltransferase activity

Inferred from direct assay PubMed 4909560. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 234234Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_0000207217

Secondary structure

.............................................. 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8P1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 8C725890D42ABF6F

FASTA23426,619
        10         20         30         40         50         60 
MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF SPGDPILWWS 

        70         80         90        100        110        120 
PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE GCASDREEGT WITRGVVEAY 

       130        140        150        160        170        180 
HRLHELGHAH SIEVWREDEL VGGMYGVAQG TLFCGESMFS RMENASKTAL LVFCEEFIGH 

       190        200        210        220        230 
GGKLIDCQVL NDHTASLGAC EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate."
Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.
J. Biol. Chem. 266:16491-16498(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat."
Shrader T.E., Tobias J.W., Varshavsky A.
J. Bacteriol. 175:4364-4374(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure."
Abramochkin G., Shrader T.E.
J. Biol. Chem. 270:20621-20628(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63145 Genomic DNA. Translation: AAC36910.1.
L10383 Unassigned DNA. Translation: AAA03231.1.
U00096 Genomic DNA. Translation: AAC73971.1.
AP009048 Genomic DNA. Translation: BAA35605.1.
PIRA36888.
RefSeqNP_415405.1. NC_000913.3.
YP_489157.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CXAX-ray1.60A1-234[»]
2DPSX-ray2.40A/B1-234[»]
2DPTX-ray2.75A/B1-234[»]
2Z3KX-ray2.85A/B2-234[»]
2Z3LX-ray2.75A/B2-234[»]
2Z3MX-ray2.70A/B2-234[»]
2Z3NX-ray2.50A/B2-234[»]
2Z3OX-ray2.40A/B2-234[»]
2Z3PX-ray2.50A/B2-234[»]
ProteinModelPortalP0A8P1.
SMRP0A8P1. Positions 2-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48235N.
IntActP0A8P1. 10 interactions.
STRING511145.b0885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73971; AAC73971; b0885.
BAA35605; BAA35605; BAA35605.
GeneID12930994.
945490.
KEGGecj:Y75_p0857.
eco:b0885.
PATRIC32116979. VBIEscCol129921_0914.

Organism-specific databases

EchoBASEEB1103.
EcoGeneEG11112. aat.

Phylogenomic databases

eggNOGCOG2360.
HOGENOMHOG000102325.
KOK00684.
OMAWSPDPRG.
OrthoDBEOG6WX4R3.
PhylomeDBP0A8P1.

Enzyme and pathway databases

BioCycEcoCyc:EG11112-MONOMER.
ECOL316407:JW0868-MONOMER.
MetaCyc:EG11112-MONOMER.

Gene expression databases

GenevestigatorP0A8P1.

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...

Other

EvolutionaryTraceP0A8P1.
PROP0A8P1.

Entry information

Entry nameLFTR_ECOLI
AccessionPrimary (citable) accession number: P0A8P1
Secondary accession number(s): P23885
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 76 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene