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P67588 (SYW_ECOL6) 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:
Tryptophan--tRNA ligase

EC=6.1.1.2
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name=TrpRS
Gene names
Name:trpS
Ordered Locus Names:c4154
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP-Rule MF_00140

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00140

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00140.

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_processtryptophanyl-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

tryptophan-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136629

Regions

Motif12 – 209"HIGH" region HAMAP-Rule MF_00140
Motif195 – 1995"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site1981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P67588 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: DEB972FAFDAF3E28

FASTA33437,424
        10         20         30         40         50         60 
MTKPIVFSGA QPSGELTIGN YMGALRQWVN MQDDYHCIYC IVDQHAITVR QDAQKLRKAT 

        70         80         90        100        110        120 
LDTLALYLAC GIDPEKSTIF VQSHVPEHAQ LGWALNCYTY FGELSRMTQF KDKSARYAEN 

       130        140        150        160        170        180 
INAGLFDYPV LMAADILLYQ TNLVPVGEDQ KQHLELSRDI AQRFNALYGD IFKVPEPFIP 

       190        200        210        220        230        240 
KSGARVMSLL EPTKKMSKSD DNRNNVIGLL EDPKSVVKKI KRAVTDSDEP PVVRYDVQNK 

       250        260        270        280        290        300 
AGVSNLLDIL SAVTGQSIPE LEKQFEGKMY GHLKGEVADA VSGMLTELQE RYHRFRNDEA 

       310        320        330 
FLQQVMKDGA EKASAHASRT LKAVYEAIGF VAKP 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82592.1.
RefSeqNP_756018.1. NC_004431.1.

3D structure databases

ProteinModelPortalP67588.
SMRP67588. Positions 4-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c4154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN82592; AAN82592; c4154.
GeneID1036689.
KEGGecc:c4154.
PATRIC18286054. VBIEscCol75197_3903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000059940.
KOK01867.
OMALLNCYTY.
OrthoDBEOG686NJQ.

Enzyme and pathway databases

BioCycECOL199310:C4154-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00140_B. Trp_tRNA_synth_B.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
IPR024109. Trp-tRNA-ligase_bac-type.
[Graphical view]
PANTHERPTHR10055. PTHR10055. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01039. TRNASYNTHTRP.
TIGRFAMsTIGR00233. trpS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYW_ECOL6
AccessionPrimary (citable) accession number: P67588
Secondary accession number(s): Q8X832
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
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