Q3K3R5 (SYE_STRA1) 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:	SAK_0165

Organism

Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700) [Complete proteome] [HAMAP]

Taxonomic identifier

205921 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup Ia

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-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. HAMAP-Rule MF_00022
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00022.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence ABA45477.1 differs from that shown. Reason: Erroneous initiation.

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 – 484	484	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_0000237407
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	255 – 259	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	258	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3K3R5 [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 867D06E1D632E906	FASTA	484	55,540
	10 20 30 40 50 60 MANKIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGDFV IRIEDTDRKR HVEDGERSQL 70 80 90 100 110 120 ENLRWLGMDW DESPETHENY RQSERLELYQ RYIDQLLAEG KAYKSYVTEE ELAAERERQE 130 140 150 160 170 180 LAGETPRYIN EFIGMSETEK EAYIAEREAA GIIPTVRLAV SESGIYKWTD MVKGDIEFEG 190 200 210 220 230 240 SNIGGDWVIQ KKDGYPTYNF AVVIDDHVMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPQ 250 260 270 280 290 300 FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYMSEAV FNFIALLGWN PGGEEEIFSR 310 320 330 340 350 360 EQLINLFDEN RLSKSPAAFD QKKMDWMSND YLKNADFESV FALCKPFLEE AGRLTDKAEK 370 380 390 400 410 420 LVELYKPQLK SADEIVPLTD LFFADFPELT EAEKEVMAAE TVPTVLSVFK EKLVSLSDEE 430 440 450 460 470 480 FTRDTIFPQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPDTIYLLGK EKSVQHIDNM LAKL

References

[1]

"Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial 'pan-genome'." Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D., Hauser C.R., Sundaram J.P. , Nelson W.C., Madupu R., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27591 / A909 / CDC SS700.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000114 Genomic DNA. Translation: ABA45477.1. Different initiation.
RefSeq	YP_328838.1. NC_007432.1.
3D structure databases
ProteinModelPortal	Q3K3R5.
ModBase	Search...
Protein-protein interaction databases
STRING	205921.SAK_0165.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA45477; ABA45477; SAK_0165.
GeneID	3685670.
KEGG	sak:SAK_0165.
PATRIC	19631530. VBIStrAga82541_0112.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K09698.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	SAGA205921:GHD7-165-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_STRA1

Accession

Primary (citable) accession number: Q3K3R5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 24, 2009
Last modified:	May 29, 2013
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program