Q10765 (SYI_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoleucine--tRNA ligase
EC=6.1.1.5

Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS

Gene names

Name:	ileS
Ordered Locus Names:	Rv1536, MT1587
ORF Names:	MTCY48.29c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	1041 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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). Ref.3
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 process	Antibiotic resistance Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucyl-tRNA aminoacylation Inferred from mutant phenotype Ref.3. Source: MTBBASE regulation of translational fidelity Inferred from electronic annotation. Source: GOC response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from direct assay PubMed 15525680. Source: MTBBASE cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 14532352. Source: MTBBASE
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activity Inferred from mutant phenotype Ref.3. Source: MTBBASE 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 – 1041	1041	Isoleucine--tRNA ligase HAMAP-Rule MF_02003		PRO_0000098550
Regions
	Motif	53 – 63	11	"HIGH" region HAMAP-Rule MF_02003
	Motif	619 – 623	5	"KMSKS" region HAMAP-Rule MF_02003
Sites
	Binding site	622	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10765 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: B5023822848E08C6	FASTA	1,041	117,340
	10 20 30 40 50 60 MTDNAYPKLA GGAPDLPALE LEVLDYWSRD DTFRASIARR DGAPEYVFYD GPPFANGLPH 70 80 90 100 110 120 YGHLLTGYVK DIVPRYRTMR GYKVERRFGW DTHGLPAELE VERQLGITDK SQIEAMGIAA 130 140 150 160 170 180 FNDACRASVL RYTDEWQAYV TRQARWVDFD NDYKTLDLAY MESVIWAFKQ LWDKGLAYEG 190 200 210 220 230 240 YRVLPYCWRD ETPLSNHELR MDDDVYQSRQ DPAVTVGFKV VGGQPDNGLD GAYLLVWTTT 250 260 270 280 290 300 PWTLPSNLAV AVSPDITYVQ VQAGDRRFVL AEARLAAYAR ELGEEPVVLG TYRGAELLGT 310 320 330 340 350 360 RYLPPFAYFM DWPNAFQVLA GDFVTTDDGT GIVHMAPAYG EDDMVVAEAV GIAPVTPVDS 370 380 390 400 410 420 KGRFDVTVAD YQGQHVFDAN AQIVRDLKTQ SGPAAVNGPV LIRHETYEHP YPHCWRCRNP 430 440 450 460 470 480 LIYRSVSSWF VRVTDFRDRM VELNQQITWY PEHVKDGQFG KWLQGARDWS ISRNRYWGTP 490 500 510 520 530 540 IPVWKSDDPA YPRIDVYGSL DELERDFGVR PANLHRPYID ELTRPNPDDP TGRSTMRRIP 550 560 570 580 590 600 DVLDVWFDSG SMPYAQVHYP FENLDWFQGH YPGDFIVEYI GQTRGWFYTL HVLATALFDR 610 620 630 640 650 660 PAFKTCVAHG IVLGFDGQKM SKSLRNYPDV TEVFDRDGSD AMRWFLMASP ILRGGNLIVT 670 680 690 700 710 720 EQGIRDGVRQ VLLPLWNTYS FLALYAPKVG TWRVDSVHVL DRYILAKLAV LRDDLSESME 730 740 750 760 770 780 VYDIPGACEH LRQFTEALTN WYVRRSRSRF WAEDADAIDT LHTVLEVTTR LAAPLLPLIT 790 800 810 820 830 840 EIIWRGLTRE RSVHLTDWPA PDLLPSDADL VAAMDQVRDV CSAASSLRKA KKLRVRLPLP 850 860 870 880 890 900 KLIVAVENPQ LLRPFVDLIG DELNVKQVEL TDAIDTYGRF ELTVNARVAG PRLGKDVQAA 910 920 930 940 950 960 IKAVKAGDGV INPDGTLLAG PAVLTPDEYN SRLVAADPES TAALPDGAGL VVLDGTVTAE 970 980 990 1000 1010 1020 LEAEGWAKDR IRELQELRKS TGLDVSDRIR VVMSVPAERE DWARTHRDLI AGEILATDFE 1030 1040 FADLADGVAI GDGVRVSIEK T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryote-like and resistant to a eubacterial-specific antisynthetase drug." Sassanfar M., Kranz J.E., Gallant P., Schimmel P., Shiba K. Biochemistry 35:9995-10003(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, RESISTANCE TO MUPIROCIN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842577 Genomic DNA. Translation: CAA98326.1. AE000516 Genomic DNA. Translation: AAK45854.1. AL123456 Genomic DNA. Translation: CCP44300.1.
PIR	E70760.
RefSeq	NP_216052.1. NC_000962.3. NP_336040.1. NC_002755.2. YP_006514924.1. NC_018143.1.
3D structure databases
ProteinModelPortal	Q10765.
SMR	Q10765. Positions 12-828.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv1536.
Proteomic databases
PRIDE	Q10765.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK45854; AAK45854; MT1587.
GeneID	13320134. 886412. 924357.
KEGG	mtc:MT1587. mtu:Rv1536.
PATRIC	18125259. VBIMycTub22151_1744.
Organism-specific databases
TubercuList	Rv1536.
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246403.
KO	K01870.
OMA	SRSRYWG.
ProtClustDB	PRK06039.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02003. Ile_tRNA_synth_type2.
InterPro	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]
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_MYCTU

Accession

Primary (citable) accession number: Q10765
Secondary accession number(s): L0T8J7, O06181

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program