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Q0SNE1 (SYE_BORAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:BAPKO_0381, BafPKo_0371
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length490 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 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001875

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2541ATP By similarity

Experimental info

Sequence conflict4791N → I in AEL69597. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q0SNE1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A4441D298C9F7779

FASTA49056,815
        10         20         30         40         50         60 
MGIRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYF SEAENDLYSS 

        70         80         90        100        110        120 
LKWLGISFDE GPVVGGDYAP YVQSQRSAIY KRYAEYLIES GHAYYCYCSP ERLERIKKIQ 

       130        140        150        160        170        180 
NINKMPPGYD RHCRNLSDEE IENVLIKKIK PVVRFKIPLE GDTSFDDVLL GKITWSNKDI 

       190        200        210        220        230        240 
SPDPVILKSD GLPTYHLANV VDDYLMKITH VLRAQEWVSS GPLHTLLYKA FKWNPPIYCH 

       250        260        270        280        290        300 
LPMVMGNDGQ KLSKRHGSTA LRQFIEDGYL PEAIINYITL LGWSYDDKRE FFSKSDLEKF 

       310        320        330        340        350        360 
FSIEKINKSP AIFDYHKLDF FNSYYIREKK DEDLFNLLLP FFQKKGYVSK PNTLEESQKL 

       370        380        390        400        410        420 
KLLVPLIKSR IKKLSDALSM TKFFYEDIKS WNLDEFLGRK KTAKEVCSIL ELIKPILEGF 

       430        440        450        460        470        480 
EKRSLEENDK IFYDFAKNNG FKLGEILLPI RIAVLGSKVS PPLFDSLKLI GKSKVFERNK 

       490 
LAQEFLRINE 

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.
[2]"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000395 Genomic DNA. Translation: ABH01637.1.
CP002933 Genomic DNA. Translation: AEL69597.1.
RefSeqYP_005592587.1. NC_017238.1.
YP_709813.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SNE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390236.BAPKO_0381.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH01637; ABH01637; BAPKO_0381.
AEL69597; AEL69597; BafPKo_0371.
GeneID12159325.
4227560.
KEGGbaf:BAPKO_0381.
bafz:BafPKo_0371.
PATRIC37189046. VBIBorAfz3878_0435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

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_BORAP
AccessionPrimary (citable) accession number: Q0SNE1
Secondary accession number(s): G0IS16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 61 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