Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P41368 (SYI2_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Synonyms:mupR
Encoded onPlasmid
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1024 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_02003

Confers high-level resistance to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis. HAMAP-Rule MF_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm HAMAP-Rule MF_02003.

Domain

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. HAMAP-Rule MF_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
   Biological processAntibiotic resistance
Protein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termPlasmid
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10241024Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098562

Regions

Motif42 – 5211"HIGH" region HAMAP-Rule MF_02003
Motif585 – 5895"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5881ATP By similarity

Experimental info

Sequence conflict5191P → R Ref.2
Sequence conflict591 – 5933GNV → ETF in CAA42080. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P41368 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 56ECD232CA0C8430

FASTA1,024118,876
        10         20         30         40         50         60 
MTKKYLNTQN EISAFWNTQK IFKKSIDNRK GQESFVFYDG PPTANGLPHA GHVLGRVIKD 

        70         80         90        100        110        120 
LVARLKTMQG FYVERKAGWD THGLPVELEV EKKIGIKGKQ DIEKYGIENF INECKKSVFN 

       130        140        150        160        170        180 
YEKEWRDFSK DLGYWVDMDS PYITLENNYI ESVWNILSTF HKKGLLYKGH KVTPYCTHDQ 

       190        200        210        220        230        240 
TALSSHEVAQ GYKNVKDLSA VVKFQLTNSK DTYFLSWTTT PWTLPANVAL AINKDLNYSK 

       250        260        270        280        290        300 
IRVENEYYIL ATDLINSIIT EKYEIIDTFS GSNLINLKYI PPFESDGLVN AYYVVDGEFV 

       310        320        330        340        350        360 
TNSEGTGIVH IAPAHGEDDY QLVLERDLDF LNVITREGVY NDRFPELVGN KAKNSDIEII 

       370        380        390        400        410        420 
KLLSKKQLLY KKQKYEHNYP HCWRCGNPLI YYAMEGWFIK TTNFKNEIIN NNNNIEWFPS 

       430        440        450        460        470        480 
HIKEGRMGNF LENMVDWNIG RNRYWGTPLN VWICNDCNHE YAPSSIKDLQ NNSINKIDED 

       490        500        510        520        530        540 
IELHRPYVDN ITLSCPKCNG KMSRVEEVID VWFDSGSMPF AQHHYPFDNQ KIFNQHFPAD 

       550        560        570        580        590        600 
FIAEGVDQTR GWFYSLLVIS TILKGKSSYK RALSLGHILD SNGKKMSKSK GNVINPTELI 

       610        620        630        640        650        660 
NKYGADSLRW ALISDSAPWN NKRFSENIVA QTKSKFIDTL DNIYKFYNMY NKIDHYNPNN 

       670        680        690        700        710        720 
EITKSRNTLD NWALSRLNTL IKESNIYVNN YDFTSAARLI NEYTNTISNW YIGDSRGRFW 

       730        740        750        760        770        780 
EQGISNDKKD AYNTLYEILT TLSRLVAPFV PFISEKIHYN LTGKSVHLQD YPQYKESFIN 

       790        800        810        820        830        840 
QALEDEMHTV IKIVELSRQA RKNADLKIKQ PLSKMVIKPN SQLNLSFLPN YYSIIKDELN 

       850        860        870        880        890        900 
IKNIELTDNI NDYITYELKL NFSSVGPKLG NKTKNIQTLI DSLSEYDKKS LIESNNFKSL 

       910        920        930        940        950        960 
SSDAELTKDD FIIKTLPKDS YQLSEDNDCV ILLDKNLSPE LIREGHAREL IRLIQQLRKK 

       970        980        990       1000       1010       1020 
KNLPINQRID IYIGVTGELL ESIKTNKNMF KENFVIKNIH LNVIDEYENT IHFNNKEIKI 


SLLY 

« Hide

References

[1]"Molecular characterization of the gene encoding high-level mupirocin resistance in Staphylococcus aureus J2870."
Hodgson J.E., Curnock S.P., Dyke K.G.H., Morris R., Sylvester D.R., Gross M.S.
Antimicrob. Agents Chemother. 38:1205-1208(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: J2870.
[2]"Cloning of the gene conferring resistance to mupirocin in Staphylococcus aureus."
Dyke K.G.H., Curnock S.P., Golding M., Noble W.C.
FEMS Microbiol. Lett. 61:195-198(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 504-519 AND 550-609.
Strain: J2870.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75439 Genomic DNA. Translation: CAA53189.1.
X59478 Genomic DNA. Translation: CAA42080.1.
X59477 Genomic DNA. Translation: CAA42079.1.
RefSeqYP_001653102.1. NC_010279.1.

3D structure databases

ProteinModelPortalP41368.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5857592.

Phylogenomic databases

eggNOGCOG0060.
ProtClustDBPRK06039.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. 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]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI2_STAAU
AccessionPrimary (citable) accession number: P41368
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries