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P00956

- SYI_ECOLI

UniProt

P00956 - SYI_ECOLI

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Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. isoleucyl-tRNA aminoacylation Source: EcoCyc
  2. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10492. ileS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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.

Expressioni

Gene expression databases

GenevestigatoriP00956.

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.
OMAiKPVHWCL.
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.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_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.
YP_488332.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73137; AAC73137; b0026.
BAB96595; BAB96595; BAB96595.
GeneIDi12932381.
944761.
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 .
PIRi B64723. SYECIT.
RefSeqi NP_414567.1. NC_000913.3.
YP_488332.1. NC_007779.1.

3D structure databases

ProteinModelPortali P00956.
SMRi P00956. Positions 3-882.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849163. 1 interaction.
DIPi DIP-10017N.
IntActi P00956. 16 interactions.
MINTi MINT-1232480.
STRINGi 511145.b0026.

Chemistry

BindingDBi P00956.
ChEMBLi CHEMBL3657.

Proteomic databases

PaxDbi P00956.
PRIDEi P00956.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73137 ; AAC73137 ; b0026 .
BAB96595 ; BAB96595 ; BAB96595 .
GeneIDi 12932381.
944761.
KEGGi ecj:Y75_p0026.
eco:b0026.
PATRICi 32115143. VBIEscCol129921_0023.

Organism-specific databases

EchoBASEi EB0487.
EcoGenei EG10492. ileS.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246402.
InParanoidi P00956.
KOi K01870.
OMAi KPVHWCL.
OrthoDBi EOG644ZM1.
PhylomeDBi P00956.

Enzyme and pathway databases

BioCyci EcoCyc:ILES-MONOMER.
ECOL316407:JW0024-MONOMER.
MetaCyc:ILES-MONOMER.

Miscellaneous databases

PROi P00956.

Gene expression databases

Genevestigatori P00956.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPi MF_02002. Ile_tRNA_synth_type1.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00392. ileS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 157 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