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Reviewed, UniProtKB/Swiss-Prot P0A8P1 (LFTR_ECOLI)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00688

Catalytic activity

L-leucyl-tRNA + protein = tRNA + L-leucyl-protein. HAMAP MF_00688

L-phenylalanyl-tRNA + protein = tRNA + L-phenylalanyl-protein. HAMAP MF_00688

Subunit structure

Monomer. HAMAP MF_00688

Subcellular location

Cytoplasm. HAMAP MF_00688

Sequence similarities

Belongs to the L/F-transferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

leucyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8P1-1 [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: 1909328] [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: 8331068] [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: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 7657641] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_001515.1.
NP_415405.1.

3D structure databases

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[»]
ModBaseSearch...

Genome annotation databases

GeneID945490.
GenomeReviewsGene locus JW0868 in contig AP009048_GR.
Gene locus b0885 in contig U00096_GR.
KEGGecj:JW0868.
eco:b0885.

Organism-specific databases

EchoBASEEB1103.
EcoGeneEG11112. aat.
CMRSearch...

Phylogenomic databases

HOGENOMP0A8P1.
OMAP0A8P1. MFYGESM.

Enzyme and pathway databases

BioCycEcoCyc:EG11112-MON.

Family and domain databases

HAMAPMF_00688.
[Tree]
InterProIPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
ProDomPD022844. Aat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00667. aat. 1 hit.
ProtoNetSearch...

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: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents