Reviewed, UniProtKB/Swiss-Prot P41368 (SYI2_STAAU)

Names and origin

Protein names

Recommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS

Gene names

Name:	ileS
Synonyms:	mupR

Encoded on

Plasmid

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	1024 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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. 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 MF_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02003
Cofactor	Zinc By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP 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.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
Biological process	Antibiotic resistance Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Plasmid
Gene Ontology (GO)
Biological process	isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1024	1024	Isoleucyl-tRNA synthetase HAMAP MF_02003		PRO_0000098562
Regions
	Motif	42 – 52	11	"HIGH" region HAMAP MF_02003
	Motif	585 – 589	5	"KMSKS" region HAMAP MF_02003
Sites
	Binding site	588	1	ATP By similarity
Experimental info
	Sequence conflict	519	1	P → R Ref.2
	Sequence conflict	591 – 593	3	GNV → ETF in CAA42080. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P41368-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 56ECD232CA0C8430	FASTA	1,024	118,876
	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

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: 8067768] [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: 1903747] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 504-519 AND 550-609. Strain: J2870.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X75439 Genomic DNA. Translation: CAA53189.1. X59478 Genomic DNA. Translation: CAA42080.1. X59477 Genomic DNA. Translation: CAA42079.1.
RefSeq	YP_001653102.1.
3D structure databases
HSSP	HSSP built from PDB template 1ILE based on UniProtKB P56690.
ModBase	Search...
Genome annotation databases
GeneID	5857592.
Enzyme and pathway databases
BRENDA	6.1.1.5. 95.
Family and domain databases
HAMAP	MF_02003. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI2_STAAU

Accession

Primary (citable) accession number: P41368

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)