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O52914 (SYE2_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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
Synonyms:gltX1
Ordered Locus Names:Cj1288c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length463 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
Reference 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 – 463463Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119531

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O52914 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: D60A0032963E6BED

FASTA46353,059
        10         20         30         40         50         60 
MHEKLTTRFA PSPTGYLHIG GLRTALYNYL YARKNGGNFL LRIEDTDLKR NSKEATKAII 

        70         80         90        100        110        120 
EAFKWCGLEH DGEVTYQSER FDLYKEYVKK LLDEGKAYYC YMSKEELEEL RAKQEAAKER 

       130        140        150        160        170        180 
PRYDGRYREF TGTPPQGIEP VVRIKAPQSG EIVFEDGVKG EVRFKAEDIM DDFIIARSDG 

       190        200        210        220        230        240 
TPTYNFTVVI DDALMGVSDV IRGDDHLSNT PKQIVLYEAL GFKIPKFFHV AMIHGEDGKK 

       250        260        270        280        290        300 
LSKRHGATDV MEYKEMGILP QALLNFLVRL GWSHGDDEVF SLEDLKKLFD PYHINKSASC 

       310        320        330        340        350        360 
YNAKKLEWLN AHYIKTLPFE EINRQLKDLG FDLSVYEKAG FLLDLLRERA KTLHDIINGA 

       370        380        390        400        410        420 
KSIVNAPQNY DENAVQKFVN KNNLELLQAF ANTLKDQKTG KDFEDFTNDF LEKKEAKLKD 

       430        440        450        460 
LAQPIRIALT GSAVSPSIFE VLEFLGVDEC KKRIDNFLKV RGK 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.
[2]Woesten M.M.S.M., Boeve M., Koot M.G.A., Nuenen A.C., van der Zeijst B.A.M.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
Strain: 129108.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35402.1.
AJ002027 Genomic DNA. Translation: CAA05150.1.
PIRA81337.
RefSeqYP_002344678.1. NC_002163.1.

3D structure databases

ProteinModelPortalO52914.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO52914. 32 interactions.
STRING192222.Cj1288c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35402; CAL35402; Cj1288c.
GeneID905580.
KEGGcje:Cj1288c.
PATRIC20059540. VBICamJej33762_1270.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1261-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_CAMJE
AccessionPrimary (citable) accession number: O52914
Secondary accession number(s): Q0P8W9, Q9PN11
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 93 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