Q03IP7 (SYE_STRTD) 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:	STER_1793

Organism

Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9) [Complete proteome] [HAMAP]

Taxonomic identifier

322159 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	484 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 – 484	484	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000001976
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022_B
	Motif	255 – 259	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	258	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03IP7 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 9EEC854C0ECF93F1	FASTA	484	55,354
	10 20 30 40 50 60 MAKDIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGTFI IRIEDTDRKR HVEDGERSQL 70 80 90 100 110 120 DNLRWLGIDW DESPETHENY RQSERLPLYQ KYIDQLLAEG KAYKSYVTEE ELAAERERQE 130 140 150 160 170 180 AAGETPRYIN EFLGMTEEEK AAYIAEREAA GIIPTVRLAV NESGIYKWHD IVKGDIEFEG 190 200 210 220 230 240 GNIGGDWVIQ KRDGYPTYNF AVVVDDHDMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPE 250 260 270 280 290 300 FGHMTLITNS ETGKKLSKRD TNTLQFIEDY RKKGYLPEAV FNFIALLGWN PGGEDEIFSR 310 320 330 340 350 360 EELIKLFDEN RLSKSPAAFD QKKLDWMSND YIKHADFDKV FALCKPFLEE AGRLTDKAEK 370 380 390 400 410 420 LVELYKPQMT AAEEIVPLTD LFFEDFPELT AAEKEVMAGE TVPTVLEAFK AKLEAMSDDE 430 440 450 460 470 480 FVTENIFSQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPETIFLLGR EKSIKHIDQV LATL

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-491 / LMD-9.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000419 Genomic DNA. Translation: ABJ66925.1.
RefSeq	YP_821121.1. NC_008532.1.
3D structure databases
ProteinModelPortal	Q03IP7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03IP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000060828; EBSTRP00000056484; EBSTRG00000060818.
GeneID	4437592.
GenomeReviews	Gene locus STER_1793 in contig CP000419_GR.
KEGG	ste:STER_1793.
PATRIC	19800981. VBIStrThe129203_1831.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
GeneTree	EBGT00050000027201.
HOGENOM	HBG628189.
OMA	DKETAND.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	STHE322159:STER_1793-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_STRTD

Accession

Primary (citable) accession number: Q03IP7

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