B0SKQ2 (SYE_LEPBP) 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:	LEPBI_I0677

Organism

Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) [Complete proteome] [HAMAP]

Taxonomic identifier

456481 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	517 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 MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00022_B.
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
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 517	517	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000367700
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP MF_00022_B
	Motif	250 – 254	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	107	1	Zinc By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	134	1	Zinc By similarity
	Metal binding	136	1	Zinc By similarity
	Binding site	253	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0SKQ2 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 01F51E9F307E26D0	FASTA	517	58,314
	10 20 30 40 50 60 MTEVRTRFAP SPSGFLHVGG ARTALFNYLY AKAKKGKFLL RIEDTDQDRS TEASFKIILE 70 80 90 100 110 120 SLKWLGMEWD EGPGVGGPNG PYTQSERIHI YKEYTDKLIQ EKKAYRCFCT AEELEGKKKQ 130 140 150 160 170 180 ADAMGIPYIY DGKCSDLSDA EIGSQLEKKI PFTVRFKTPH KIVIVDDMIQ GKVKFESKLI 190 200 210 220 230 240 GDFIIVKSDG FPSYNYAVVI DDALMKITHV IRGVGHLSNT PRQILIFEAF GFPLPRFAHA 250 260 270 280 290 300 SEIVGTDGKK LSKRAGATSV LAFRDLGYSS ETMRNYMALL GWTSPDGKEY MSDEELCSVF 310 320 330 340 350 360 DVERCSKSPA TFDVFKKLKE EEKESVDFNK LTILGLAEYL NPKSKLNWMS NKYIRDTKIE 370 380 390 400 410 420 TLGKALEPFL KDCQIPEAFK SGENPQLLSI LDSVRVYLDR LIQAPPYIEE FFLENLSFEN 430 440 450 460 470 480 DEAKQLVLEG KGKEVVAEFY RIVKESSLTT PDAYKESMAK VGEITGEKGR TLFMPIRAIT 490 500 510 TGKSHGLELP ILFSLLGQEK MVKRMEQLAG ILGISLR

References

[1]

"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis." Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. , Davies J.K., Medigue C., Adler B. PLoS ONE 3:E1607-E1607(2008) [PubMed: 18270594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Patoc 1 / ATCC 23582 / Paris.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000786 Genomic DNA. Translation: ABZ96809.1.
RefSeq	YP_001838085.1. NC_010602.1.
3D structure databases
ProteinModelPortal	B0SKQ2.
ModBase	Search...
Protein-protein interaction databases
STRING	B0SKQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6224229.
GenomeReviews	Gene locus LEPBI_I0677 in contig CP000786_GR.
KEGG	lbi:LEPBI_I0677.
PATRIC	22348068. VBILepBif123590_0682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628189.
OMA	LLYPCYE.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LBIF456481:LEPBI_I0677-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
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-synth_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]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K09698.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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_LEPBP

Accession

Primary (citable) accession number: B0SKQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program