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P67593 (SYW_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:SA0855
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 329329Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136677

Regions

Motif10 – 189"HIGH" region HAMAP-Rule MF_00140
Motif193 – 1975"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site1961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P67593 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 5F55F1B897FA0291

FASTA32936,909
        10         20         30         40         50         60 
METLFSGIQP SGIPTIGNYI GALKQFVDVQ NDYDCYFCIV DQHAITMPQD RLKLRKQTRQ 

        70         80         90        100        110        120 
LAAIYLASGI DPDKATLFIQ SEVPAHVQAG WMLTTIASVG ELERMTQYKD KAQKAVEGIP 

       130        140        150        160        170        180 
AGLLTYPPLM AADIVLYNTN IVPVGDDQKQ HIELTRNLVD RFNSRYNDVL VKPEIRMPKV 

       190        200        210        220        230        240 
GGRVMSLQDP TRKMSKSDDN AKNFISLLDE PNVAAKKIKS AVTDSDGIIK FDRDNKPGIT 

       250        260        270        280        290        300 
NLISIYAGLT DMPIKDIEAK YEGEGYGKFK GDLAEIVKAF LVEFQEKYES FYNSDKLDDI 

       310        320 
LDQGRDKAHK VSFKTVKKME KAMGLGRKR 

« Hide

References

[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB42096.1.
PIRE89867.
RefSeqNP_374118.1. NC_002745.2.

3D structure databases

ProteinModelPortalP67593.
SMRP67593. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA0855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB42096; BAB42096; BAB42096.
GeneID1123672.
KEGGsau:SA0855.
PATRIC19573878. VBIStaAur116463_0911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000059940.
KOK01867.
OMAGWGQFKP.
OrthoDBEOG686NJQ.
ProtClustDBPRK00927.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-901-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_STAAN
AccessionPrimary (citable) accession number: P67593
Secondary accession number(s): Q99V94
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 62 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