Q73FE5 (TILS_BACC1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA(Ile)-lysidine synthase
EC=6.3.4.19

Alternative name(s):
tRNA(Ile)-2-lysyl-cytidine synthase
tRNA(Ile)-lysidine synthetase

Gene names

Name:	tilS
Ordered Locus Names:	BCE_0061

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine By similarity. HAMAP-Rule MF_01161
Catalytic activity	(tRNA(Ile2))-cytidine34 + L-lysine + ATP = (tRNA(Ile2))-lysidine34 + AMP + diphosphate + H2O. HAMAP-Rule MF_01161
Subcellular location	Cytoplasm By similarity.
Domain	The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. HAMAP-Rule MF_01161
Sequence similarities	Belongs to the tRNA(Ile)-lysidine synthase family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	tRNA modification Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP ligase activity, forming carbon-nitrogen bonds 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 – 476	476	tRNA(Ile)-lysidine synthase HAMAP-Rule MF_01161		PRO_0000181642
Regions
	Nucleotide binding	30 – 35	6	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q73FE5 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 8BF17437F3481BC0	FASTA	476	54,969
	10 20 30 40 50 60 MKDTFVEKVD DFVKQHDVLK ERSTIVVGVS GGPDSVALLY YLLEKRAAKQ FEIVVAHVDH 70 80 90 100 110 120 MFRGDESHED LQFVQDLCKE LGVICETIRI NVSQYQQQYG MNAQVAAREC RYAFLERIMK 130 140 150 160 170 180 KYDARYVALG HHGDDQVETI LMRLVRGSTP KGYAGIAVKR PFHNGYLIRP LLGVTKEEIV 190 200 210 220 230 240 DYCHKLKIIP RIDPSNKKEV YTRNRLRKYV LPHLKEENPQ VHEKFQKFSM QMQEDEAYLQ 250 260 270 280 290 300 ELAFEKMNKV ITKKSDKQIS LSIPAFESMS MPLQRRGIQL ILNYLYEYKI PSSLSSIHID 310 320 330 340 350 360 KVIEFFKRTQ PSGSLDFPGD LKIVRAYEEC SFGFKQEIVS PFLQDLSVPG TITLSNGDKL 370 380 390 400 410 420 VTEVSEDIPS NMNETVFVAK YNDISYPLRI RSRENGDRMS IQGMNGTKKI KAIFIEAKVP 430 440 450 460 470 REKREEWPVV CDARGNVIWL PLLKRSAFAI SKETAKKDKY MIIHYKSKES SGRIMK

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS38997.1.
RefSeq	NP_976389.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q73FE5.
ModBase	Search...
Protein-protein interaction databases
STRING	222523.BCE_0061.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS38997; AAS38997; BCE_0061.
GeneID	2748948.
KEGG	bca:BCE_0061.
PATRIC	18848942. VBIBacCer118379_0058.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0037.
HOGENOM	HOG000236506.
KO	K04075.
OMA	NDISYPL.
ProtClustDB	CLSK886565.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_01161. tRNA(Ile)-lys_synt.
InterPro	IPR012094. Lysidine-tRNA-synth. IPR012796. Lysidine-tRNA-synth_C. IPR012795. Lysidine-tRNA-synth_N. IPR015262. Lysidine-tRNA-synth_subst-bd. IPR020825. Phe-tRNA_synthase_B3/B4. IPR014729. Rossmann-like_a/b/a_fold. IPR011063. tRNA-lysidine/thiocyt_synth. [Graphical view]
PANTHER	PTHR11807:SF2. PTHR11807:SF2. 1 hit.
Pfam	PF01171. ATP_bind_3. 1 hit. PF09179. TilS. 1 hit. PF11734. TilS_C. 1 hit. [Graphical view]
SMART	SM00977. TilS_C. 1 hit. [Graphical view]
SUPFAM	SSF56037. B3_4. 1 hit.
TIGRFAMs	TIGR02433. lysidine_TilS_C. 1 hit. TIGR02432. lysidine_TilS_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TILS_BACC1

Accession

Primary (citable) accession number: Q73FE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program