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B6JLN1 (SYE2_HELP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:HPP12_0656
OrganismHelicobacter pylori (strain P12) [Complete proteome] [HAMAP]
Taxonomic identifier570508 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367686

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif232 – 2365"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6JLN1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: F14F51734B7BECC1

FASTA43951,062
        10         20         30         40         50         60 
MLRFAPSPTG DMHIGNLRAA IFNYIVAKQQ HKPFLIRIED TDKERNIEGK DREILEILKL 

        70         80         90        100        110        120 
MGISWDKLVY QSHNIDYHRE MAEKLLKENK AFYCYASAEF LEREKEKAKN EKRPFRYLDE 

       130        140        150        160        170        180 
WATLEKDKNH APVVRLKAPN HAVSFNDAIK KEVKFEPDEL DSFVLLRQDK SPTYNFACAC 

       190        200        210        220        230        240 
DDLLYEISLI IRGEDHVSNT PKQILIQQAL GLNDPIVYAH LPIILDETSG KKMSKRDEAS 

       250        260        270        280        290        300 
SVKWLLNQGF LPVAIGNYLI TIGNKVPKEV FSLDEAIEWF SLENLSSSPA HFNLKYLKHL 

       310        320        330        340        350        360 
NHEHLKLLDD EKLLELTLIK DKNLLGLLRL FIEECGTLLE LKEKISLFLE PKDIVKTYEN 

       370        380        390        400        410        420 
EDFKERCLAL FNALKSMDFQ AYKDFESFKK EAMRLSQLKG KDFFKPLRIL LTGNSHGVEL 

       430 
PLIFPYIQSH HQEVLRLKA 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain P12."
Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001217 Genomic DNA. Translation: ACJ07809.1.
RefSeqYP_002301289.1. NC_011498.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570508.HPP12_0656.

Proteomic databases

PRIDEB6JLN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ07809; ACJ07809; HPP12_0656.
GeneID7009790.
KEGGhpp:HPP12_0656.
PATRIC20609292. VBIHelPyl2824_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAHHAPVVR.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12410.

Enzyme and pathway databases

BioCycHPYL570508:GJ8D-670-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_HELP2
AccessionPrimary (citable) accession number: B6JLN1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries