Q8G0E8 (SYE2_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2

Gene names

Name:	gltX2
Synonyms:	gltX1
Ordered Locus Names:	BR1147, BS1330_I1143

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	473 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
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 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete 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 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 – 473	473	Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022		PRO_0000119524
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	240 – 244	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	243	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G0E8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: CBDF287970001020	FASTA	473	51,981
	10 20 30 40 50 60 MSKPVITRFA PSPTGYLHIG GARTALFNWL YAKHCGGKML LRIEDTDRER STEAATAAIL 70 80 90 100 110 120 DGLTWLGLDW DGEAISQFER APRHREVAEE LVANGKAYYC YASPEELEEM REKARAEGRP 130 140 150 160 170 180 PRYDGRWRDR DPSEAPAGVK PVIRIKAPRD GETVVHDAVQ GDVRFPNKDL DDFIILRSDG 190 200 210 220 230 240 TPTYMHAVVV DDHDMGVTHI IRGGDHLTNA ARQTIIYNAM GWDVPQMSHI SLIHGADGAK 250 260 270 280 290 300 LSKRHGALGV DAYRAMGYLP AALRNYLVRL GWSHGDDEIM STEQMIEWFD VKDINKGAAR 310 320 330 340 350 360 FDFQKLEAIN GLYMRSSDDQ ALFDALVAVL PEIEGGKELA EALDDKGRAQ LLLAMPGLKE 370 380 390 400 410 420 RAKTLVELAD GAKFIFASRP LALDEKAASL LNDEGRAVLK PVYPVLEAVG EWTAESLDAA 430 440 450 460 470 IRAHAEAEGL KLGKIAQPLR AALTGRATSP GVFDVLVVLG REESLARIGD QIG

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30067.1. CP002997 Genomic DNA. Translation: AEM18485.1.
RefSeq	NP_698152.1. NC_004310.3. YP_005615977.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8G0E8.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR1147.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN30067; AAN30067; BR1147. AEM18485; AEM18485; BS1330_I1143.
GeneID	1166823. 12138176.
KEGG	bms:BR1147. bsi:BS1330_I1143.
PATRIC	17790627. VBIBruSui107850_1167.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	RYRDFKG.
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

SYE2_BRUSU

Accession

Primary (citable) accession number: Q8G0E8
Secondary accession number(s): G0KA69

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program