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A1A9C8

- LFTR_ECOK1

UniProt

A1A9C8 - LFTR_ECOK1

Protein

Leucyl/phenylalanyl-tRNA--protein transferase

Gene

aat

Organism
Escherichia coli O1:K1 / APEC
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
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    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

    1. leucyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein catabolic process Source: InterPro

    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:Ecok1_07740
    ORF Names:APECO1_1204
    OrganismiEscherichia coli O1:K1 / APEC
    Taxonomic identifieri405955 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000008216: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 234234Leucyl/phenylalanyl-tRNA--protein transferasePRO_0000304335Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi405955.APECO1_1204.

    Structurei

    3D structure databases

    ProteinModelPortaliA1A9C8.
    SMRiA1A9C8. Positions 2-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG2360.
    HOGENOMiHOG000102325.
    KOiK00684.
    OMAiWSPDPRG.
    OrthoDBiEOG6WX4R3.

    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.

    A1A9C8-1 [UniParc]FASTAAdd to Basket

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    MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF    50
    SPGDPILWWS PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE 100
    GCASDREEGT WITRGVVEAY HRLHELGHAH SIEVWREDEL VGGMYGVAQG 150
    TLFCGESMFS RMENASKTAL LVFCDEFIRH GGKLIDCQVL NDHTASLGAC 200
    EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE 234
    Length:234
    Mass (Da):26,704
    Last modified:January 23, 2007 - v1
    Checksum:i79724D84D52ABE74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ00268.1.
    RefSeqiYP_851982.1. NC_008563.1.

    Genome annotation databases

    EnsemblBacteriaiABJ00268; ABJ00268; APECO1_1204.
    GeneIDi4491899.
    KEGGiecv:APECO1_1204.
    PATRICi18213136. VBIEscCol127180_0856.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ00268.1 .
    RefSeqi YP_851982.1. NC_008563.1.

    3D structure databases

    ProteinModelPortali A1A9C8.
    SMRi A1A9C8. Positions 2-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405955.APECO1_1204.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ00268 ; ABJ00268 ; APECO1_1204 .
    GeneIDi 4491899.
    KEGGi ecv:APECO1_1204.
    PATRICi 18213136. VBIEscCol127180_0856.

    Phylogenomic databases

    eggNOGi COG2360.
    HOGENOMi HOG000102325.
    KOi K00684.
    OMAi WSPDPRG.
    OrthoDBi EOG6WX4R3.

    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

    1. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
      Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
      J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiLFTR_ECOK1
    AccessioniPrimary (citable) accession number: A1A9C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 53 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3