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Q8L1B1

- SYI2_PSEFL

UniProt

Q8L1B1 - SYI2_PSEFL

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Protein

Isoleucine--tRNA ligase 2

Gene

ileS2

Organism
Pseudomonas fluorescens
Status
Reviewed - Annotation score: 4 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) (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

Zn2+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
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

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-HAMAP
Complete GO annotation...

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

        10         20         30         40         50
MSTEGSGPVR FPAMEDAVLE RWEKEKTFEQ SISAREGKPV YVFYDGPPFA
60 70 80 90 100
TGLPHYGHIL TSYIKDVIPR YQTMLGKQVP RRWGWDCHGL PVEFEVEKAM
110 120 130 140 150
GFKSKRDILE FGVEQFNDEC RELVLKYADD WRGFVNRMGR WVDFDGAYKT
160 170 180 190 200
MDNDYMESVL WGFKTLHDKG HVYEGGKIVP YCVRCQTVLS NFEARLDDAF
210 220 230 240 250
RPRRDMSAYV KFRQQDRPDT FFLAWTTTPW TLPANVALAV AADENYVCIE
260 270 280 290 300
HGEERLWLAE GCLGGLFDEP VILERCTGAE LAGLRYLPVV GEVIDASAHR
310 320 330 340 350
VVTADFVQMG DGSGIVHIAP AFGEDDALLG QQYELPAPNP VRDDGTFSDA
360 370 380 390 400
VAQYAGQNIF EATPRILADL KSSGLLFKQE QIEHNYPHCW RCDNPLIYRA
410 420 430 440 450
VESWFIRASA LREQLVENNS QVNWVPEHVK EGRFGDWIRN ARDWAVSRNR
460 470 480 490 500
FWGAPIPVWR CDQCGTVEVM GSIAQIEARS GRKVEDLHVP HIDEHRFACQ
510 520 530 540 550
CCEGTMSRVT GVFDCWFESG AMPFASRHYP FENKQEFEQT FPADFIVEYL
560 570 580 590 600
AQTRGWFYTM MVISTGCFEQ NPFKNAMCHG VILAKDGRKM SKRLKNYPNP
610 620 630 640 650
MDLMQTHGSD ALRVALLASP VCKGEDIKFS EESVRDVVRR YHLLFWNCLQ
660 670 680 690 700
FYKTFTEIDQ FSPSGDLGQP LDNVLDHYLL HELAALESDI KMWMESLDFS
710 720 730 740 750
KIYSRIEVFI NVLSTWYLRL NKARIWRDGL DDDKRQCYEV LHYALSNFAR
760 770 780 790 800
LLAPFMPFLA EAVYTELGYA DSVHLQDWPS IDRQYLSYEL ADEMSSLRNL
810 820 830 840 850
IASVRNVRET NGVSQKFPLR SIRVAGIEQA VLERYAQFLE EELNVKQVQW
860 870 880 890 900
AADADEWAQP VVVLIFSLLG KRLGPAMKAV TTAVKAGEYV IDEQGGLVAA
910 920 930 940 950
GQTIQPHEFE RRLTVRDTLN NVGIVENMVV WLDLDIDASL KREGAVRELN
960 970 980 990 1000
RRLQDLRKKA KLGYTEKVDI AVLGGAYVDE ILVHHEDWLK SQLLVQSLLR
1010 1020 1030
SDLEAPLAVD EVELPEGDPV RIQLRRSVLA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 65 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