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A1USG2 (SYE2_BARBK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:BARBAKC583_0607
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length456 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 – 456456Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367611

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1USG2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 4DDEF66D17BB0E25

FASTA45652,506
        10         20         30         40         50         60 
MIKVRFAPSP TGYIHIGNTR IALFNWLYAQ ANNGTFILRY DDTDLERSKQ EYIDGIMTDL 

        70         80         90        100        110        120 
EWLDIKPDEI HHQSKRFSRY DKVAETLKER GLLYPCYETV EELGRHRKIQ LSRKLPPVYD 

       130        140        150        160        170        180 
RRALKLTKED KRLLESQGRK PHWRFLLPNF ESNPFQIKRT EISWDDIVKG KQTIDLASIS 

       190        200        210        220        230        240 
DPVLIREDGS YLYTLPSVID DIDMAITHII RGEDHITNTG AQITIFEALN AKLPAFGHIN 

       250        260        270        280        290        300 
LLTTVSGQGL SKRNSDLSIC SLREEGFESM AVRCLSVLTG TSKNIEAHRD QKALLEHFSL 

       310        320        330        340        350        360 
QNTSKSAAKF DITDLISLNS HFVHELTYEE VKTRLEKLSI CGEKAEYFWN TIRDNIDKVN 

       370        380        390        400        410        420 
DAALWWEIIH SDQSFDAVSF EDRAFLQQSV DLLPEGSLND ESWKIWTTAL KEKTDRKGKA 

       430        440        450 
LFMSLRLALT GRQHGPEMGK LLPLLGREKI INRLTI 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35685 / KC583.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000524 Genomic DNA. Translation: ABM44944.1.
RefSeqYP_988915.1. NC_008783.1.

3D structure databases

ProteinModelPortalA1USG2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360095.BARBAKC583_0607.

Proteomic databases

PRIDEA1USG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM44944; ABM44944; BARBAKC583_0607.
GeneID4684716.
KEGGbbk:BARBAKC583_0607.
PATRIC20537499. VBIBarBac6912_0593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAGRLYPC.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycBBAC360095:GHRY-607-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_BARBK
AccessionPrimary (citable) accession number: A1USG2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 55 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