Q055X5 (SYE_LEPBL) 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:	LBL_0256

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]

Taxonomic identifier

355276 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	521 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
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm 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 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: 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 521	521	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000001919
Regions
	Motif	13 – 23	11	"HIGH" region HAMAP MF_00022_B
	Motif	253 – 257	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q055X5 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: E19F802C89CAA148	FASTA	521	58,931
	10 20 30 40 50 60 MNQNREVRTR FAPSPSGFLH VGGARTALFN YLYAKSQGGK FILRIEDTDQ NRSTEDSFKI 70 80 90 100 110 120 ILESLKWLGV RWDEGPEIGG EYGPYIQSQR LDIYKEYTEK LLKEKKAYRC FCTQEELEAK 130 140 150 160 170 180 KKQAEAMGVP YVYDGLHANM SDEEVEEKLK QKIPYSIRFK TPSKTLIVDD IIQGKVKFET 190 200 210 220 230 240 KLIGDFIIVK SDGFPSYNYA VVVDDALMKI THVIRGVGHL SNTPRQILLY EALDYEIPEF 250 260 270 280 290 300 AHASEIVGMD GKKLSKRAGA TSILAFRDLG YLPETFRNYM ALLGWTSSDG REFLPEGELE 310 320 330 340 350 360 KIFDVHRCSK SPSTFDVFKK PKGGEDEVVT NFSDLTQIAE AMNPKSKLNW LSNRTIRDLK 370 380 390 400 410 420 ISKVLESLLP FLKDRKDIPE EVKNINSPAL TSIIESIRVY LDNLAQAPDY IAEFFVTDLK 430 440 450 460 470 480 IQSQEATGFM KDGDGPKVVK EFYGILKNSD PKTDENYKDL MSKVGEVTGQ KGKTLYMPIR 490 500 510 520 VATTGKSVGL ELPILFPLLG KEKLLQRIEK TAKEAGIPLS T

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L550.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000348 Genomic DNA. Translation: ABJ77870.1.
RefSeq	YP_796803.1. NC_008508.1.
3D structure databases
ProteinModelPortal	Q055X5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q055X5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4407455.
GenomeReviews	Gene locus LBL_0256 in contig CP000348_GR.
KEGG	lbl:LBL_0256.
PATRIC	22363682. VBILepBor75619_0320.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	VRFRMPD.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	LBOR355276:LBL_0256-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	K01885.
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_LEPBL

Accession

Primary (citable) accession number: Q055X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program