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Protein

Isoleucine--tRNA ligase

Gene

ileS

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

Functioni

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Kineticsi

  1. KM=5 µM for isoleucine1 Publication
  2. KM=0.4 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei561 – 5611Aminoacyl-adenylateBy similarity
    Binding sitei605 – 6051ATPBy similarity
    Metal bindingi901 – 9011ZincBy similarity
    Metal bindingi904 – 9041ZincBy similarity
    Metal bindingi921 – 9211ZincBy similarity
    Metal bindingi924 – 9241ZincBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • isoleucyl-tRNA aminoacylation Source: EcoCyc
    • response to antibiotic Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Antibiotic resistance, Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:ILES-MONOMER.
    ECOL316407:JW0024-MONOMER.
    MetaCyc:ILES-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase
    Short name:
    IleRS
    Gene namesi
    Name:ileS
    Synonyms:ilvS
    Ordered Locus Names:b0026, JW0024
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10492. ileS.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 941G → R: 6000-fold increase in Km for isoleucine and 4-fold increase in Km for ATP, with no effect on activity. 1 Publication
    Mutagenesisi97 – 971C → S: No effect on activity. 1 Publication
    Mutagenesisi102 – 1021I → N: No significant effect on activity. 1 Publication
    Mutagenesisi183 – 1831K → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-421. 1 Publication
    Mutagenesisi241 – 2411T → A: Nearly the same editing activity as the wild-type. 1 Publication
    Mutagenesisi242 – 2421T → A: Abolishes editing activity against valine, with little change in aminoacylation activity; when associated with A-250. 1 Publication
    Mutagenesisi242 – 2421T → P: Abolishes editing activity against valine, with little change in aminoacylation activity. 1 Publication
    Mutagenesisi243 – 2431T → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications
    Mutagenesisi243 – 2431T → R: Abolishes pretransfer editing. 2 Publications
    Mutagenesisi246 – 2461T → A: Nearly the same editing activity as the wild-type. 1 Publication
    Mutagenesisi250 – 2501N → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications
    Mutagenesisi333 – 3331H → A: Alters the specificity for hydrolysis of the aminoacyl tRNA ester, with no effect on pretransfer editing. 1 Publication
    Mutagenesisi342 – 3421D → A or N: Strong decrease in total editing and deacylation activities. Severely deficient in translocation from the aminoacylation site to the editing site. 1 Publication
    Mutagenesisi342 – 3421D → E: Reduces 2- to 3-fold the total editing activity and 2-fold the deacylation activity. Moderately reduces translocation from the aminoacylation site to the editing site. 1 Publication
    Mutagenesisi421 – 4211W → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-183. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 938937Isoleucine--tRNA ligasePRO_0000098384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00956.
    PRIDEiP00956.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi849163. 1 interaction.
    DIPiDIP-10017N.
    IntActiP00956. 16 interactions.
    MINTiMINT-1232480.
    STRINGi511145.b0026.

    Structurei

    3D structure databases

    ProteinModelPortaliP00956.
    SMRiP00956. Positions 3-882.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi602 – 6065"KMSKS" region

    Domaini

    IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0060.
    HOGENOMiHOG000246402.
    InParanoidiP00956.
    KOiK01870.
    OMAiVLGDWDN.
    OrthoDBiEOG644ZM1.
    PhylomeDBiP00956.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00956-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT
    60 70 80 90 100
    FILHDGPPYA NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL
    110 120 130 140 150
    PIELKVEQEY GKPGEKFTAA EFRAKCREYA ATQVDGQRKD FIRLGVLGDW
    160 170 180 190 200
    SHPYLTMDFK TEANIIRALG KIIGNGHLHK GAKPVHWCVD CRSALAEAEV
    210 220 230 240 250
    EYYDKTSPSI DVAFQAVDQD ALKAKFAVSN VNGPISLVIW TTTPWTLPAN
    260 270 280 290 300
    RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE
    310 320 330 340 350
    LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG
    360 370 380 390 400
    LETANPVGPD GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ
    410 420 430 440 450
    HSYPCCWRHK TPIIFRATPQ WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA
    460 470 480 490 500
    RIESMVANRP DWCISRQRTW GVPMSLFVHK DTEELHPRTL ELMEEVAKRV
    510 520 530 540 550
    EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST HSSVVDVRPE
    560 570 580 590 600
    FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG
    610 620 630 640 650
    RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD
    660 670 680 690 700
    SYRRIRNTAR FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL
    710 720 730 740 750
    KAYEAYDFHE VVQRLMRFCS VEMGSFYLDI IKDRQYTAKA DSVARRSCQT
    760 770 780 790 800
    ALYHIAEALV RWMAPILSFT ADEVWGYLPG EREKYVFTGE WYEGLFGLAD
    810 820 830 840 850
    SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV TLYAEPELSA
    860 870 880 890 900
    KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK
    910 920 930
    CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA
    Length:938
    Mass (Da):104,297
    Last modified:January 23, 2007 - v5
    Checksum:i238CEDAF461F01D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 26422TPWTL…DYALV → RRGLCLPTAQSLLHQISTMR WW AA sequence (PubMed:6390679).CuratedAdd
    BLAST
    Sequence conflicti300 – 3012EL → DV AA sequence (PubMed:6390679).Curated
    Sequence conflicti587 – 5871R → C AA sequence (PubMed:6390679).Curated
    Sequence conflicti637 – 6371E → Q AA sequence (PubMed:6390679).Curated
    Sequence conflicti724 – 7241G → V AA sequence (PubMed:6390679).Curated
    Sequence conflicti738 – 7381A → P AA sequence (PubMed:6390679).Curated
    Sequence conflicti740 – 7434ADSV → RTVW AA sequence (PubMed:6390679).Curated
    Sequence conflicti787 – 7871F → L AA sequence (PubMed:6390679).Curated
    Sequence conflicti830 – 8301K → N AA sequence (PubMed:6390679).Curated
    Sequence conflicti867 – 8693GAT → DRRY AA sequence (PubMed:6390679).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti594 – 5941F → L in strain: PS102.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73137.1.
    AP009048 Genomic DNA. Translation: BAB96595.2.
    M10428 Genomic DNA. Translation: AAA24606.1.
    X00776 Genomic DNA. Translation: CAA25352.1.
    K01990 Genomic DNA. Translation: AAA24091.1.
    PIRiB64723. SYECIT.
    RefSeqiNP_414567.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73137; AAC73137; b0026.
    BAB96595; BAB96595; BAB96595.
    GeneIDi944761.
    KEGGiecj:Y75_p0026.
    eco:b0026.
    PATRICi32115143. VBIEscCol129921_0023.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73137.1.
    AP009048 Genomic DNA. Translation: BAB96595.2.
    M10428 Genomic DNA. Translation: AAA24606.1.
    X00776 Genomic DNA. Translation: CAA25352.1.
    K01990 Genomic DNA. Translation: AAA24091.1.
    PIRiB64723. SYECIT.
    RefSeqiNP_414567.1. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP00956.
    SMRiP00956. Positions 3-882.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi849163. 1 interaction.
    DIPiDIP-10017N.
    IntActiP00956. 16 interactions.
    MINTiMINT-1232480.
    STRINGi511145.b0026.

    Chemistry

    BindingDBiP00956.
    ChEMBLiCHEMBL3657.

    Proteomic databases

    PaxDbiP00956.
    PRIDEiP00956.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73137; AAC73137; b0026.
    BAB96595; BAB96595; BAB96595.
    GeneIDi944761.
    KEGGiecj:Y75_p0026.
    eco:b0026.
    PATRICi32115143. VBIEscCol129921_0023.

    Organism-specific databases

    EchoBASEiEB0487.
    EcoGeneiEG10492. ileS.

    Phylogenomic databases

    eggNOGiCOG0060.
    HOGENOMiHOG000246402.
    InParanoidiP00956.
    KOiK01870.
    OMAiVLGDWDN.
    OrthoDBiEOG644ZM1.
    PhylomeDBiP00956.

    Enzyme and pathway databases

    BioCyciEcoCyc:ILES-MONOMER.
    ECOL316407:JW0024-MONOMER.
    MetaCyc:ILES-MONOMER.

    Miscellaneous databases

    PROiP00956.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase."
      Webster T., Tsai H., Kula M., Mackie G.A., Schimmel P.
      Science 226:1315-1317(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase."
      Yanagisawa T., Lee J.T., Wu H.C., Kawakami M.
      J. Biol. Chem. 269:24304-24309(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11 AND 606-615.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and PS102.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    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], SEQUENCE REVISION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon."
      Kamio Y., Lin C.-K., Regue M., Wu H.C.
      J. Biol. Chem. 260:5616-5620(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
    7. "Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli."
      Yu F., Yamada H., Daishima K., Mizushima S.
      FEBS Lett. 173:264-268(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-938.
    8. "Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene."
      Innis M.A., Tokunaga M., Williams M.E., Loranger J.M., Chang S.-Y., Chang S., Wu H.C.
      Proc. Natl. Acad. Sci. U.S.A. 81:3708-3712(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 795-938.
    9. "Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure."
      Clarke N.D., Lien D.C., Schimmel P.
      Science 240:521-523(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-94; CYS-97 AND ILE-102, KINETIC PARAMETERS.
    10. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    11. "Enzyme structure with two catalytic sites for double-sieve selection of substrate."
      Nureki O., Vassylyev D.G., Tateno M., Shimada A., Nakama T., Fukai S., Konno M., Hendrickson T.L., Schimmel P., Yokoyama S.
      Science 280:578-582(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-241; THR-243; THR-246 AND ASN-250.
    12. "Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis."
      Nomanbhoy T.K., Hendrickson T.L., Schimmel P.
      Mol. Cell 4:519-528(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: EDITING ACTIVITY.
    13. "Errors from selective disruption of the editing center in a tRNA synthetase."
      Hendrickson T.L., Nomanbhoy T.K., Schimmel P.
      Biochemistry 39:8180-8186(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-242 AND ASN-250.
    14. "Mutational separation of two pathways for editing by a class I tRNA synthetase."
      Hendrickson T.L., Nomanbhoy T.K., de Crecy-Lagard V., Fukai S., Nureki O., Yokoyama S., Schimmel P.
      Mol. Cell 9:353-362(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-243 AND HIS-333, PRESENCE OF TWO EDITING SUBSITES.
    15. "Blocking site-to-site translocation of a misactivatd amino acid by mutation of a class I tRNA synthetase."
      Bishop A.C., Nomanbhoy T.K., Schimmel P.
      Proc. Natl. Acad. Sci. U.S.A. 99:585-590(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-342, TRANSLOCATION OF MISACTIVATED VALINE.
    16. "Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase."
      Bishop A.C., Beebe K., Schimmel P.R.
      Proc. Natl. Acad. Sci. U.S.A. 100:490-494(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-183 AND TRP-421.
    17. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-183, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiSYI_ECOLI
    AccessioniPrimary (citable) accession number: P00956
    Secondary accession number(s): P78038, Q59429
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 161 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Strain PS102 is resistant to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.