Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8L1B1

- SYI2_PSEFL

UniProt

Q8L1B1 - SYI2_PSEFL

Protein

Isoleucine--tRNA ligase 2

Gene

ileS2

Organism
Pseudomonas fluorescens
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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) By similarity.By similarity
    Confers high-level resistance to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog produced by P.fluorescens NCIMB 10586 itself that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.

    Catalytic activityi

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

    Cofactori

    Zinc.By similarity

    Kineticsi

    1. KM=10 µM for isoleucine
    2. KM=330 µM for ATP

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei592 – 5921ATPBy 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: UniProtKB-HAMAP
    2. response to antibiotic Source: UniProtKB-KW

    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

    BRENDAi6.1.1.5. 5121.
    SABIO-RKQ8L1B1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase 2 (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase 2
    Short name:
    IleRS 2
    Gene namesi
    Name:ileS2
    Synonyms:mupM
    OrganismiPseudomonas fluorescens
    Taxonomic identifieri294 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10301029Isoleucine--tRNA ligase 2PRO_0000098556Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L1B1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi48 – 5811"HIGH" regionAdd
    BLAST
    Motifi589 – 5935"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)) By similarity.By similarity

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02003. Ile_tRNA_synth_type2.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023586. Ile-tRNA-ligase_type2.
    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.
    [Graphical view]
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 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.

    Q8L1B1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTEGSGPVR FPAMEDAVLE RWEKEKTFEQ SISAREGKPV YVFYDGPPFA     50
    TGLPHYGHIL TSYIKDVIPR YQTMLGKQVP RRWGWDCHGL PVEFEVEKAM 100
    GFKSKRDILE FGVEQFNDEC RELVLKYADD WRGFVNRMGR WVDFDGAYKT 150
    MDNDYMESVL WGFKTLHDKG HVYEGGKIVP YCVRCQTVLS NFEARLDDAF 200
    RPRRDMSAYV KFRQQDRPDT FFLAWTTTPW TLPANVALAV AADENYVCIE 250
    HGEERLWLAE GCLGGLFDEP VILERCTGAE LAGLRYLPVV GEVIDASAHR 300
    VVTADFVQMG DGSGIVHIAP AFGEDDALLG QQYELPAPNP VRDDGTFSDA 350
    VAQYAGQNIF EATPRILADL KSSGLLFKQE QIEHNYPHCW RCDNPLIYRA 400
    VESWFIRASA LREQLVENNS QVNWVPEHVK EGRFGDWIRN ARDWAVSRNR 450
    FWGAPIPVWR CDQCGTVEVM GSIAQIEARS GRKVEDLHVP HIDEHRFACQ 500
    CCEGTMSRVT GVFDCWFESG AMPFASRHYP FENKQEFEQT FPADFIVEYL 550
    AQTRGWFYTM MVISTGCFEQ NPFKNAMCHG VILAKDGRKM SKRLKNYPNP 600
    MDLMQTHGSD ALRVALLASP VCKGEDIKFS EESVRDVVRR YHLLFWNCLQ 650
    FYKTFTEIDQ FSPSGDLGQP LDNVLDHYLL HELAALESDI KMWMESLDFS 700
    KIYSRIEVFI NVLSTWYLRL NKARIWRDGL DDDKRQCYEV LHYALSNFAR 750
    LLAPFMPFLA EAVYTELGYA DSVHLQDWPS IDRQYLSYEL ADEMSSLRNL 800
    IASVRNVRET NGVSQKFPLR SIRVAGIEQA VLERYAQFLE EELNVKQVQW 850
    AADADEWAQP VVVLIFSLLG KRLGPAMKAV TTAVKAGEYV IDEQGGLVAA 900
    GQTIQPHEFE RRLTVRDTLN NVGIVENMVV WLDLDIDASL KREGAVRELN 950
    RRLQDLRKKA KLGYTEKVDI AVLGGAYVDE ILVHHEDWLK SQLLVQSLLR 1000
    SDLEAPLAVD EVELPEGDPV RIQLRRSVLA 1030
    Length:1,030
    Mass (Da):117,875
    Last modified:January 23, 2007 - v3
    Checksum:i2D930693BE1DC935
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti175 – 1751G → R in AAL85500. (PubMed:12652905)Curated
    Sequence conflicti400 – 4001A → T in AAM12927. 1 PublicationCurated
    Sequence conflicti667 – 6671L → P in AAM12927. 1 PublicationCurated
    Sequence conflicti671 – 6711L → P in AAM12927. 1 PublicationCurated
    Sequence conflicti717 – 7171Y → H in AAM12927. 1 PublicationCurated
    Sequence conflicti805 – 8051R → C in AAM12927. 1 PublicationCurated
    Sequence conflicti886 – 8861A → V in AAM12927. 1 PublicationCurated
    Sequence conflicti939 – 9391S → P in AAM12927. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY079084 Genomic DNA. Translation: AAL85500.1.
    AF318063 Genomic DNA. Translation: AAM12927.1.
    AB062785 Genomic DNA. Translation: BAC07171.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY079084 Genomic DNA. Translation: AAL85500.1 .
    AF318063 Genomic DNA. Translation: AAM12927.1 .
    AB062785 Genomic DNA. Translation: BAC07171.1 .

    3D structure databases

    ProteinModelPortali Q8L1B1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 6.1.1.5. 5121.
    SABIO-RK Q8L1B1.

    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_02003. Ile_tRNA_synth_type2.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023586. Ile-tRNA-ligase_type2.
    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.
    [Graphical view ]
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 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

    1. "Analysis of rILERS, an isoleucyl-tRNA synthetase gene associated with mupirocin production by Pseudomonas fluorescens NCIMB 10586."
      Rangaswamy V., Hernandez-Guzman G., Shufran K.A., Bender C.L.
      DNA Seq. 13:343-351(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49323 / NCIMB 10586.
    2. "Nucleotide sequence of a 75 kb region of the chromosome of Pseudomonas fluorescens NCIMB 10586 required for biosynthesis of the polyketide antibiotic mupirocin."
      El-Sayed A.K., Hothersall J., Cooper S.M., Stephens E., Thomas C.M.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49323 / NCIMB 10586.
    3. "How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid? Evidence for two evolutionarily distinct isoleucyl-tRNA synthetases conferring self-defense."
      Yanagisawa T., Kawakami M.
      J. Biol. Chem. 278:25887-25894(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, RESISTANCE TO MUPIROCIN.
      Strain: ATCC 49323 / NCIMB 10586.

    Entry informationi

    Entry nameiSYI2_PSEFL
    AccessioniPrimary (citable) accession number: Q8L1B1
    Secondary accession number(s): Q8GM72, Q8RL58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 63 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    P.fluorescens NCIMB 10586 possesses two distinct IleRSs (IleRS-R1 and IleRS-R2), each with a different level of sensitivity to mupirocin. Purified IleRs-R2 shows no sensitivity to mupirocin even at a concentration of 5 mM, 100'000 fold higher than the Ki value of IleRS-R1.

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3