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A4W496 (SYE_STRS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:SSU98_2027
OrganismStreptococcus suis (strain 98HAH33) [Complete proteome] [HAMAP]
Taxonomic identifier391296 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length484 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.

Sequence caution

The sequence ABP93185.1 differs from that shown. Reason: Erroneous initiation.

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 – 484484Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000331000

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4W496 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 9FDF590B1F402C17

FASTA48455,533
        10         20         30         40         50         60 
MTKPIRVRYA PSPTGLLHIG NARTALFNYL FARHHGGTFL IRIEDTDRKR HVEDGERSQL 

        70         80         90        100        110        120 
ENLRWLGIDW DESPETHENY RQSERLDIYQ KYVDQLLAEG KAYKSYVTEE ELAAERERQE 

       130        140        150        160        170        180 
AAGETPRYIN EYLGMSEDEK TAYIAEREAA GIVPTVRLAV NEAGIYKWND IVKGEIEFEG 

       190        200        210        220        230        240 
GNIGGDWVIQ KRDGYPTYNF AVVIDDYLMK ISHVIRGDDH IANTPKQLMV YEALGWEAPE 

       250        260        270        280        290        300 
FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RRKGYMPEAV FNFIGLLGWN PGGEEEIFSR 

       310        320        330        340        350        360 
EQFIQLFDEN RLSKSPAAFD QKKMDWMSNE YIKNADLETI FNLAKPFLEE AGRLTDKAEK 

       370        380        390        400        410        420 
LVELYKPQMS SADEIVGLTD LFFSDFPELT AEEKEVMAGE TVPTVLNALK EKLEAMTDED 

       430        440        450        460        470        480 
FQPDNIFPQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPNTIYLLGR EKSIQHIDNM 


LKSL 

« Hide

References

[1]"A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y. expand/collapse author list , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 98HAH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000408 Genomic DNA. Translation: ABP93185.1. Different initiation.
RefSeqYP_001201585.1. NC_009443.1.

3D structure databases

ProteinModelPortalA4W496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391296.SSU98_2027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP93185; ABP93185; SSU98_2027.
GeneID5102679.
KEGGssv:SSU98_2027.
PATRIC19780276. VBIStrSui72275_1993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSSUI391296:GI2E-2085-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 nameSYE_STRS2
AccessionPrimary (citable) accession number: A4W496
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 52 of the entry and version 2 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