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A4VY04 (SYE_STRSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:SSU05_2027
OrganismStreptococcus suis (strain 05ZYH33) [Complete proteome] [HAMAP]
Taxonomic identifier391295 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length464 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 – 464464Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367774

Regions

Motif235 – 2395"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4VY04 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 0BE49E83670FA601

FASTA46453,347
        10         20         30         40         50         60 
MPVQHCLTYL FARHHGGTFL IRIEDTDRKR HVEDGERSQL ENLRWLGIDW DESPETHENY 

        70         80         90        100        110        120 
RQSERLDIYQ KYVDQLLAEG KAYKSYVTEE ELAAERERQE AAGETPRYIN EYLGMSEDEK 

       130        140        150        160        170        180 
TAYIAEREAA GIVPTVRLAV NEAGIYKWND IVKGEIEFEG GNIGGDWVIQ KRDGYPTYNF 

       190        200        210        220        230        240 
AVVIDDYLIK ISHVIRGDDH IANTPKQLMV YEALGWEAPE FGHMTLIINS ETGKKLSKRD 

       250        260        270        280        290        300 
TNTLQFIEDY RRKGYMPEAV FNFIGLLGWN PGGEEEIFSR EQFIQLFDEN RLSKSPAAFD 

       310        320        330        340        350        360 
QKKMDWMSNE YIKNADLETI FNLAKPFLEE AGRLTDKAEK LVELYKPQMS SADEIVGLTD 

       370        380        390        400        410        420 
LFFSDFPELT AEEKEVMAGE TVPTVLNALK EKLEAMTDED FQPDNIFPQI KAVQKETGIK 

       430        440        450        460 
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: 05ZYH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000407 Genomic DNA. Translation: ABP90993.1.
RefSeqYP_001199393.1. NC_009442.1.

3D structure databases

ProteinModelPortalA4VY04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391295.SSU05_2027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP90993; ABP90993; SSU05_2027.
GeneID5099479.
KEGGssu:SSU05_2027.
PATRIC19775808. VBIStrSui128929_1996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSSUI391295:GHI8-2087-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_STRSY
AccessionPrimary (citable) accession number: A4VY04
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 54 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