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B0BC83 (SYE_CHLTB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:CTLon_0701
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length506 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 – 506506Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090065

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BC83 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 7B3AA040504EF6B5

FASTA50658,563
        10         20         30         40         50         60 
MTVQNVRVRV APSPTGDPHV GTAYMALFNE VFARKYNGQM ILRIEDTDQT RSRDDYEANI 

        70         80         90        100        110        120 
FSALKWCGIR WDEGPDVGGA YGPYRQSERT EIYKKYAEIL LQTDCAYKCF ATPQELQEMR 

       130        140        150        160        170        180 
AVASTLGYRG GYDRRYRYLS PEEVRQREEQ GQPYTIRLKV PLTGESVFED QCKGRVVFPW 

       190        200        210        220        230        240 
ADVDDQVLVK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY KAFGWEPPQF 

       250        260        270        280        290        300 
FHMPLLLNPD GSKLSKRKNP TSIFYYRDAG YKKEAFMNFL TLMGYSMEGD EEIYSMQRLI 

       310        320        330        340        350        360 
EAFDPKRIGR SGAVFDIRKL DWMNKHYLNH EGSPESLLQE LKGWLWNDEF LLKILPLCQS 

       370        380        390        400        410        420 
RITTLADFVG LTSFFFTAIP QYSKEELLPS SLKQEQAAVM LYSLVKYLEK KDLWEKDFFY 

       430        440        450        460        470        480 
QGSKWLAEAF QVHHKKAVIP LLYVAITGAK QGLPLFDSME LLGKARTRAR LTYAQNLLGG 

       490        500 
VSKKVQQQVD KALQDQPLED IRFLDF 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCH-1/proctitis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884177 Genomic DNA. Translation: CAP07098.1.
RefSeqYP_001653789.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BC83.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471473.CTLon_0701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP07098; CAP07098; CTLon_0701.
GeneID5858990.
KEGGctl:CTLon_0701.
PATRIC20383067. VBIChlTra68089_0759.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCTRA471473:GHJK-735-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_CHLTB
AccessionPrimary (citable) accession number: B0BC83
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 45 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