Skip Header

Contribute Send feedback
Read comments (?) or add your own

A9ISS8 (SYE2_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:BT_0938
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length457 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 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 By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367613

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif249 – 2535"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9ISS8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: F0BA21B87AC790B5

FASTA45752,582
        10         20         30         40         50         60 
MVKVRFAPSP TGYIHIGNIR SALFNWLYAQ AHKGEFILRY DDTDVERSKQ EYIDAIAVDL 

        70         80         90        100        110        120 
EWLGIQPDAI YYQSKRFNRY DEVAEILKQR GLLYPCYETA EELERRRKIQ LSRKLPPIYD 

       130        140        150        160        170        180 
RAALKLTAEE KKNCESQGRK PHWRFLLPNF ENDPLQTKRT EVCWNDAVKG KQTIDLASLS 

       190        200        210        220        230        240 
DPVLIREDET YLYTLPSVVD DVDMAITHII RGDDHITNTG VQIALFKALD AELPVFGHTN 

       250        260        270        280        290        300 
LLATVLGKGF SKRNNDLSIR SLREEGFESI AVQCLAVLIG TSQNVHPYPH QAALLEHFNL 

       310        320        330        340        350        360 
QDTSKSVAKF DIADLCTLNS HLVHELNYED VKTRLKNLSI EGEKAEYFWN AIRSNIDKVN 

       370        380        390        400        410        420 
EAVLWWKIIH DEQNFDAVAQ EDRAFVQQSL NFLPEGVLKD ESWQVWTTAL KEKTGRKGKS 

       430        440        450 
LFMPLRQALT GMDHGPEMGK LLQLLGREKV IERLSRK 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK01335.1.
RefSeqYP_001609330.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9ISS8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9ISS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5830092.
GenomeReviewsGene locus BT_0938 in contig AM260525_GR.
PATRIC20549632. VBIBarTri113218_0970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMALLYPCYE.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycBTRI382640:BT_0938-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. 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]
Gene3DG3DSA: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.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_BART1
AccessionPrimary (citable) accession number: A9ISS8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families