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Q4L3I7 (SYE_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:SH2481
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

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.

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_0000237405

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4L3I7 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: DACA3A30F6619E55

FASTA48456,301
        10         20         30         40         50         60 
MSERIRVRYA PSPTGYLHIG NARTALFNYL FAKHYDGDFV VRIEDTDSKR NLEDGESSQF 

        70         80         90        100        110        120 
DNLKWLGLDW DESIDKDKGY GPYRQSERGD IYNPLIQQLL DEDKAYKCYM TEEELEKERE 

       130        140        150        160        170        180 
DQIARGEMPR YGGQHAHLTE EERQQFEAEG RRPSIRFRVP QDQTYTFNDM VKGEISFDSN 

       190        200        210        220        230        240 
NIGDWVIVKK DGIPTYNFAV AIDDYYMGIS DVIRGDDHVS NTPKQLMIYE AFGWEAPRFG 

       250        260        270        280        290        300 
HMSLIVNEER KKLSKRDGQI LQFIEQYRDL GYLPEALFNF ITLLGWSPEG EEEIFSKEEF 

       310        320        330        340        350        360 
IKIFDEKRLS KSPAMFDRQK LAWVNNQYMK TKDTDTVFEL ALPHLIKANL IPESPSEDDK 

       370        380        390        400        410        420 
EWGRKLVALY QKEMSYAGEI VPLSEMFFHE MPELGEEEQE VINGEQVPEL MTHLYGKLEA 

       430        440        450        460        470        480 
LEPFEAADIK KTIKEVQKET GIKGKQLFMP IRVAVTGQMH GPELPNTIEV LGKDKVLSRL 


KKFV 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE05790.1.
RefSeqYP_254396.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L3I7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH2481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE05790; BAE05790; SH2481.
GeneID3482194.
KEGGsha:SH2481.
PATRIC19621031. VBIStaHae67511_2435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-2539-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_STAHJ
AccessionPrimary (citable) accession number: Q4L3I7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 62 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