Q5NHY6 (SYE_FRATT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Name:	gltX
Ordered Locus Names:	FTT_0307

Organism

Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) [Reference proteome] [HAMAP]

Taxonomic identifier

177416 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella › Francisella tularensis › Francisella tularensis subsp. tularensis

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	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	glutamyl-tRNA aminoacylation 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 glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000119564
Regions
	Motif	8 – 18	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	236 – 240	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Metal binding	97	1	Zinc By similarity
	Metal binding	99	1	Zinc By similarity
	Metal binding	124	1	Zinc By similarity
	Metal binding	126	1	Zinc By similarity
	Binding site	239	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5NHY6 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: B5D3AC570C11C4A2	FASTA	468	52,953
	10 20 30 40 50 60 MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ EAVDAILDGM 70 80 90 100 110 120 SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS KERLEELREY QQANNLKTGY 130 140 150 160 170 180 DGKCRDANYI PQQGESYVVR FKNPQDGVVS WDDAVKGRIS ISNHELDDMI IQRADGSPTY 190 200 210 220 230 240 NFCVVVDDID MAITHIIRGD DHVNNTPKQI NIYKALNANV PIFAHVPMIL GPDGAKLSKR 250 260 270 280 290 300 HGAVNVMQYR EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 310 320 330 340 350 360 KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV DTLVELAEKS 370 380 390 400 410 420 SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ QWQDPDVLHN IVSTTAEQCQ 430 440 450 460 VGMGKVGMPL RVAITGSGQS PDIGITLKLL GKNKVVARLT KALEELCK

References

[1]

"The complete genome sequence of Francisella tularensis, the causative agent of tularemia." Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H., Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D., Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S., Sjoestedt A. , Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W., Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W. Nat. Genet. 37:153-159(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCHU S4 / Schu 4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ749949 Genomic DNA. Translation: CAG44940.1.
RefSeq	YP_169356.1. NC_006570.2.
3D structure databases
ProteinModelPortal	Q5NHY6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5NHY6. 10 interactions.
STRING	177416.FTT_0307.
Protocols and materials databases
DNASU	3191767.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG44940; CAG44940; FTT_0307.
GeneID	3191767.
KEGG	ftu:FTT_0307.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	WENVRVR.
ProtClustDB	PRK01406.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_FRATT

Accession

Primary (citable) accession number: Q5NHY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	February 1, 2005
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program