Q97NG1 (SYE_STRPN) 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:	SP_2069

Organism

Streptococcus pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
eno	Q97QS2	2	EBI-2207733,EBI-2207206

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000119665
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)
	Q97NG1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 72EF5FDF704B3011	FASTA	486	55,961
	10 20 30 40 50 60 MSKDIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGTFL IRIEDTDRKR HVEDGERSQL 70 80 90 100 110 120 ENLRWLGMDW DESPESHENY RQSERLDLYQ KYIDQLLAEG KAYKSYVTEE ELAAERERQE 130 140 150 160 170 180 VAGETPRYIN EYLGMSEEEK AAYIAEREAA GIIPTVRLAV NESGIYKWHD MVKGDIEFEG 190 200 210 220 230 240 GNIGGDWVIQ KKDGYPTYNF AVVIDDHDMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPE 250 260 270 280 290 300 FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYLPEAV FNFIALLGWN PGGEDEIFSR 310 320 330 340 350 360 EEFIKLFDEN RLSKSPAAFD QKKLDWMSND YIKNADLETI FEMAKPFLEE AGRLTDKAEK 370 380 390 400 410 420 LVELYKPQMK SVDEIIPLTD LFFSDFPELT EAEREVMTGE TVPTVLEAFK AKLEAMTDDE 430 440 450 460 470 480 FVTENIFPQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPDTIFLLGR EKSIQHIENM LKEISK

References

[1]

"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M. Science 293:498-506(2001) [PubMed: 11463916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005672 Genomic DNA. Translation: AAK76132.1.
PIR	C95242.
RefSeq	NP_346492.1. NC_003028.3.
3D structure databases
ProteinModelPortal	Q97NG1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q97NG1. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000026661; EBSTRP00000025753; EBSTRG00000026661.
GeneID	931970.
GenomeReviews	Gene locus SP_2069 in contig AE005672_GR.
KEGG	spn:SP_2069.
PATRIC	19708723. VBIStrPne105772_2152.
TIGR	SP_2069.
Phylogenomic databases
GeneTree	EBGT00050000027201.
HOGENOM	HBG628189.
OMA	DKETAND.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	SPNE170187-1:SP_2069-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_STRPN

Accession

Primary (citable) accession number: Q97NG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program