A7GJZ9 (SYE_BACCN) 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:	Bcer98_0082

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	485 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 – 485	485	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_1000074316
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	252 – 256	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	255	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GJZ9 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: CB16F2A5299F1549	FASTA	485	55,661
	10 20 30 40 50 60 MEKQVRVRYA PSPTGHLHIG NARTALFNYL FARHQDGKFI IRIEDTDVKR NVAGGEESQL 70 80 90 100 110 120 KYLKWLGMDW DEGVDVGGKY GPYRQTERLD IYKELYEDLL ERGLAYKCYM TEEELEAERE 130 140 150 160 170 180 GQIARGETPR YAGNHRNLTE EQIAQFEAEG RVPSIRFRVP DNREYKFNDI VKGDVTFHSN 190 200 210 220 230 240 DFGDFVIVKK DGIPTYNFAV AVDDHLMEIT HVLRGDDHIS NTPKQMMIYE AFGWDTPQFG 250 260 270 280 290 300 HMTLIVNESR KKLSKRDESI IQFIEQYEAL GYLPEAIFNF IALLGWSPVG EEEIFSKDEF 310 320 330 340 350 360 IKMFDAARLS KSPALFDSQK LKWMNNQYMK KQDLDTVVAL SLPHLVKAGR VSEDLSEQEA 370 380 390 400 410 420 AWVRDVIALY HEQMSYGAEI VELSEMFFKD HVDFEEEGKE VLKGEQVPEV LRAFAVELEA 430 440 450 460 470 480 LEEVEPATIK KAIKAVQKET GHKGKNLFMP IRVATTGQTH GPELPNAIAL LGKEKVLKRI QKVIG

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS20457.1.
RefSeq	YP_001373452.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GJZ9.
ModBase	Search...
Protein-protein interaction databases
STRING	315749.Bcer98_0082.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS20457; ABS20457; Bcer98_0082.
GeneID	5344349.
KEGG	bcy:Bcer98_0082.
PATRIC	18928328. VBIBacCyt128034_0093.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K09698.
OMA	ESIIQFV.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	BCYT315749:GH2A-230-MONOMER.
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_BACCN

Accession

Primary (citable) accession number: A7GJZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program