B3CLF5 (SYE2_WOLPP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2

Gene names

Name:	gltX2
Ordered Locus Names:	WP0615

Organism

Wolbachia pipientis subsp. Culex pipiens (strain wPip) [Complete proteome] [HAMAP]

Taxonomic identifier

570417 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Wolbachieae › Wolbachia › Wolbachia endosymbiont of Culex quinquefasciatus

Protein attributes

Sequence length	450 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.
Subcellular location	Cytoplasm By similarity.
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: 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 – 450	450	Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022		PRO_0000367795
Regions
	Motif	10 – 20	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	232 – 236	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	235	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B3CLF5 [UniParc]. Last modified July 22, 2008. Version 1. Checksum: 11C4B6AB9A6A3AAE	FASTA	450	51,202
	10 20 30 40 50 60 MPGIVTRFAP SPTGFLHIGG ARTALFNWLY AQRHGGQFLL RIEDTDRKRS TQEAIDAIID 70 80 90 100 110 120 GLKWLGISYD GEIVYQSKRI DRHIEVANLL VEKGRAYHCY CPENEVAEKK IRAREEGKIY 130 140 150 160 170 180 KHKCTHSTSN AEPVVRFKVP DSEDIVVDDK IYGQVTISSD QLDDIVILRS DNTPTYIFAV 190 200 210 220 230 240 VVDDHDAGIT DIIRGSDHLT NTFKQLLIYQ ALDFDVPRFA HVPLIHGEDG NKLSKRHGAT 250 260 270 280 290 300 SVCDYEKMGI LPQAMRNYLL RLGWSHGNDE IISDEQAIEW FNLESIGRSP ARLDFKKLEH 310 320 330 340 350 360 LNNHYISNMS NEDILTLMLR ENTLTDKKKG YLLQGLTELK KRANYLTELL DLAKFYIQVD 370 380 390 400 410 420 LSEEAQQIVK SNLNVIKLLA SFLSSVGSED WNKNFLSSQI KEFSKLHNIK MSDIYHSLRA 430 440 450 PITGIMDAPG IIDIMVILGK DECIKRLQAI

References

[1]

"Genome evolution of Wolbachia strain wPip from the Culex pipiens group." Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A., Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J. Mol. Biol. Evol. 25:1877-1887(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: wPip.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM999887 Genomic DNA. Translation: CAQ54723.1.
RefSeq	YP_001975381.1. NC_010981.1.
3D structure databases
ProteinModelPortal	B3CLF5.
ModBase	Search...
Protein-protein interaction databases
STRING	570417.WPa_0615.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ54723; CAQ54723; WP0615.
GeneID	6385357.
KEGG	wpi:WPa_0615.
PATRIC	24026860. VBIWolEnd95846_0677.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
KO	K01885.
OMA	RYRDFKG.
ProtClustDB	PRK01406.
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

SYE2_WOLPP

Accession

Primary (citable) accession number: B3CLF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 22, 2008
Last modified:	May 1, 2013
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