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P0A8P1

- LFTR_ECOLI

UniProt

P0A8P1 - LFTR_ECOLI

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Protein

Leucyl/phenylalanyl-tRNA--protein transferase

Gene

aat

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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.

Catalytic activityi

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

GO - Molecular functioni

  1. leucyltransferase activity Source: EcoCyc

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process via the N-end rule pathway Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Leucyl/phenylalanyl-tRNA--protein transferase (EC:2.3.2.6)
Alternative name(s):
L/F-transferase
Leucyltransferase
Phenyalanyltransferase
Gene namesi
Name:aat
Synonyms:ycaA
Ordered Locus Names:b0885, JW0868
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11112. aat.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Leucyl/phenylalanyl-tRNA--protein transferasePRO_0000207217Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0A8P1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-48235N.
IntActiP0A8P1. 10 interactions.
STRINGi511145.b0885.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Helixi16 – 183
Turni21 – 255
Beta strandi26 – 294
Helixi35 – 439
Beta strandi57 – 593
Beta strandi62 – 676
Helixi69 – 713
Helixi76 – 838
Beta strandi88 – 936
Helixi95 – 1039
Beta strandi106 – 1083
Helixi109 – 1113
Helixi114 – 12512
Beta strandi128 – 1369
Beta strandi139 – 14911
Beta strandi152 – 16211
Helixi165 – 17915
Beta strandi184 – 1896
Helixi192 – 1965
Beta strandi200 – 2023
Helixi204 – 21411
Turni221 – 2244
Beta strandi225 – 2306

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A8P1.
SMRiP0A8P1. Positions 2-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8P1.

Family & Domainsi

Sequence similaritiesi

Belongs to the L/F-transferase family.Curated

Phylogenomic databases

eggNOGiCOG2360.
HOGENOMiHOG000102325.
InParanoidiP0A8P1.
KOiK00684.
OMAiWSPDPRG.
OrthoDBiEOG6WX4R3.
PhylomeDBiP0A8P1.

Family and domain databases

HAMAPiMF_00688. Leu_Phe_trans.
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.

P0A8P1 [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:June 7, 2005 - v1
Checksum:i8C725890D42ABF6F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63145 Genomic DNA. Translation: AAC36910.1.
L10383 Unassigned DNA. Translation: AAA03231.1.
U00096 Genomic DNA. Translation: AAC73971.1.
AP009048 Genomic DNA. Translation: BAA35605.1.
PIRiA36888.
RefSeqiNP_415405.1. NC_000913.3.
YP_489157.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73971; AAC73971; b0885.
BAA35605; BAA35605; BAA35605.
GeneIDi12930994.
945490.
KEGGiecj:Y75_p0857.
eco:b0885.
PATRICi32116979. VBIEscCol129921_0914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63145 Genomic DNA. Translation: AAC36910.1 .
L10383 Unassigned DNA. Translation: AAA03231.1 .
U00096 Genomic DNA. Translation: AAC73971.1 .
AP009048 Genomic DNA. Translation: BAA35605.1 .
PIRi A36888.
RefSeqi NP_415405.1. NC_000913.3.
YP_489157.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CXA X-ray 1.60 A 1-234 [» ]
2DPS X-ray 2.40 A/B 1-234 [» ]
2DPT X-ray 2.75 A/B 1-234 [» ]
2Z3K X-ray 2.85 A/B 2-234 [» ]
2Z3L X-ray 2.75 A/B 2-234 [» ]
2Z3M X-ray 2.70 A/B 2-234 [» ]
2Z3N X-ray 2.50 A/B 2-234 [» ]
2Z3O X-ray 2.40 A/B 2-234 [» ]
2Z3P X-ray 2.50 A/B 2-234 [» ]
ProteinModelPortali P0A8P1.
SMRi P0A8P1. Positions 2-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48235N.
IntActi P0A8P1. 10 interactions.
STRINGi 511145.b0885.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73971 ; AAC73971 ; b0885 .
BAA35605 ; BAA35605 ; BAA35605 .
GeneIDi 12930994.
945490.
KEGGi ecj:Y75_p0857.
eco:b0885.
PATRICi 32116979. VBIEscCol129921_0914.

Organism-specific databases

EchoBASEi EB1103.
EcoGenei EG11112. aat.

Phylogenomic databases

eggNOGi COG2360.
HOGENOMi HOG000102325.
InParanoidi P0A8P1.
KOi K00684.
OMAi WSPDPRG.
OrthoDBi EOG6WX4R3.
PhylomeDBi P0A8P1.

Enzyme and pathway databases

BioCyci EcoCyc:EG11112-MONOMER.
ECOL316407:JW0868-MONOMER.
MetaCyc:EG11112-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A8P1.
PROi P0A8P1.

Gene expression databases

Genevestigatori P0A8P1.

Family and domain databases

HAMAPi MF_00688. Leu_Phe_trans.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view ]
Pfami PF03588. Leu_Phe_trans. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
TIGRFAMsi TIGR00667. aat. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiLFTR_ECOLI
AccessioniPrimary (citable) accession number: P0A8P1
Secondary accession number(s): P23885
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3