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Protein

Leucyl/phenylalanyl-tRNA--protein transferase

Gene

aat

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + L-leucyl-[protein].UniRule annotation
L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein].UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Leucyl/phenylalanyl-tRNA--protein transferaseUniRule annotation (EC:2.3.2.6UniRule annotation)
Alternative name(s):
L/F-transferaseUniRule annotation
LeucyltransferaseUniRule annotation
PhenyalanyltransferaseUniRule annotation
Gene namesi
Name:aatUniRule annotation
Ordered Locus Names:BWG_0737
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002125681 – 234Leucyl/phenylalanyl-tRNA--protein transferaseAdd BLAST234

Structurei

3D structure databases

ProteinModelPortaliC4ZQ11.
SMRiC4ZQ11.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L/F-transferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000102325.
KOiK00684.
OMAiYRQGIFP.

Family and domain databases

HAMAPiMF_00688. Leu_Phe_trans. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamiPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR00667. aat. 1 hit.

Sequencei

Sequence statusi: Complete.

C4ZQ11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF
60 70 80 90 100
SPGDPILWWS PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE
110 120 130 140 150
GCASDREEGT WITRGVVEAY HRLHELGHAH SIEVWREDEL VGGMYGVAQG
160 170 180 190 200
TLFCGESMFS RMENASKTAL LVFCEEFIGH GGKLIDCQVL NDHTASLGAC
210 220 230
EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE
Length:234
Mass (Da):26,619
Last modified:July 28, 2009 - v1
Checksum:i8C725890D42ABF6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63640.1.
RefSeqiWP_001241678.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR63640; ACR63640; BWG_0737.
KEGGiebw:BWG_0737.
PATRICi18270547. VBIEscCol60876_0812.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63640.1.
RefSeqiWP_001241678.1. NC_012759.1.

3D structure databases

ProteinModelPortaliC4ZQ11.
SMRiC4ZQ11.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR63640; ACR63640; BWG_0737.
KEGGiebw:BWG_0737.
PATRICi18270547. VBIEscCol60876_0812.

Phylogenomic databases

HOGENOMiHOG000102325.
KOiK00684.
OMAiYRQGIFP.

Family and domain databases

HAMAPiMF_00688. Leu_Phe_trans. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamiPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR00667. aat. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLFTR_ECOBW
AccessioniPrimary (citable) accession number: C4ZQ11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.