Q1CTM7 (SYE2_HELPH) 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:	HPAG1_0628

Organism

Helicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]

Taxonomic identifier

357544 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	439 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 – 439	439	Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022		PRO_0000367684
Regions
	Motif	6 – 16	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)
	Q1CTM7 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: 5973F94B8B0E0F66	FASTA	439	51,177
	10 20 30 40 50 60 MLRFAPSPTG DMHIGNLRAA IFNYIVAKQQ HKPFLIRIED TDKERNIEGK DQEILEILKF 70 80 90 100 110 120 MGISWDKLVY QSHNIDYHRE MAEKLLKENK AFYCYASTEF LEREKEKAKN EKRPFRYLDE 130 140 150 160 170 180 WATLEKDKHH APVVRLKAPN HAVSFNDAIK KEVKFEPDEL DSFVLLRQDK SPTYNFACTC 190 200 210 220 230 240 DDLLYEVSLI IRGEDHVSNT PKQILIQQAL GSNDPIVYAH LPIILDEVSG KKMSKRDEAS 250 260 270 280 290 300 SVKWLLNQGF LPVAIANYLI TIGNKVPKEV FSLDEAIEWF SLENLSNSPA HFNLKYLKHL 310 320 330 340 350 360 NHEHLKLLDD EKLLKLTSIK DKNLLGLLRL FIEECGTLLE LKEKISLFLE PKDIVKTYEN 370 380 390 400 410 420 EDFKERCLAL FNALKSMDFQ VYKDFESFKK EAMRLSQLKG KDFFKPLRIL LTGNSHGVEL 430 PLIFPYIQSH YQEVLRLKA

References

[1]

"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression." Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HPAG1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000241 Genomic DNA. Translation: ABF84695.1.
RefSeq	YP_627369.1. NC_008086.1.
3D structure databases
ProteinModelPortal	Q1CTM7.
ModBase	Search...
Protein-protein interaction databases
STRING	357544.HPAG1_0628.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABF84695; ABF84695; HPAG1_0628.
GeneID	4098754.
KEGG	hpa:HPAG1_0628.
PATRIC	20602602. VBIHelPyl56048_0649.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	SVKWLLN.
ProtClustDB	PRK12410.
Enzyme and pathway databases
BioCyc	HPYL357544:GH1F-670-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

SYE2_HELPH

Accession

Primary (citable) accession number: Q1CTM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 11, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program