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P67022 (SYE_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:MW0483
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [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_0000119656

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
P67022 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 4CBA5FF08DA23EFA

FASTA48456,289
        10         20         30         40         50         60 
MSDRIRVRYA PSPTGYLHIG NARTALFNYL YAKHYNGDFV IRIEDTDKKR NLEDGETSQF 

        70         80         90        100        110        120 
DNLKWLGLDW DESVDKDNGY GPYRQSERQH IYQPLIDQLL AEDKAYKCYM TEEELEAERE 

       130        140        150        160        170        180 
AQIARGEMPR YGGQHAHLTE EQRQQFEAEG RQPSIRFRVP QNQTYSFDDM VKGNISFDSN 

       190        200        210        220        230        240 
GIGDWVIVKK DGIPTYNFAV AIDDHYMQIS DVIRGDDHIS NTPKQIMIYE AFGWEPPRFG 

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

       310        320        330        340        350        360 
IKIFDEKRLS KSPAFFDKQK LAWVNNQYMK QKDTETVFQL ALPHLIKANL IPEVPSEEDL 

       370        380        390        400        410        420 
SWGRKLIALY QKEMSYAGEI VPLSEMFFKE MPALGEEEQQ VINGEQVPEL MTHLFSKLEA 

       430        440        450        460        470        480 
LEPFEAAEIK KTIKEVQKET GIKGKQLFMP IRVAVTGQMH GPELPNTIEV LGKEKVLNRL 


KQYK 

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB94348.1.
RefSeqNP_645300.1. NC_003923.1.

3D structure databases

ProteinModelPortalP67022.
SMRP67022. Positions 5-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196620.MW0483.

Proteomic databases

PRIDEP67022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB94348; BAB94348; BAB94348.
GeneID1002594.
KEGGsam:MW0483.
PATRIC19567498. VBIStaAur44266_0511.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-504-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_STAAW
AccessionPrimary (citable) accession number: P67022
Secondary accession number(s): Q99W75
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 63 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