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Q8XD57 (SYK1_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. 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:
Lysine--tRNA ligase

EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS
Gene names
Name:lysS
Ordered Locus Names:Z4228, ECs3762
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP-Rule MF_00252

Cofactor

Binds 3 magnesium ions per subunit By similarity. HAMAP-Rule MF_00252

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00252

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00252.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlysyl-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

lysine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 505504Lysine--tRNA ligase HAMAP-Rule MF_00252
PRO_0000152624

Sites

Metal binding4151Magnesium 1 By similarity
Metal binding4221Magnesium 1 By similarity
Metal binding4221Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XD57 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CDABF71FAC12A629

FASTA50557,631
        10         20         30         40         50         60 
MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH AEFDGKENEE 

        70         80         90        100        110        120 
LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD 

       130        140        150        160        170        180 
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES 

       190        200        210        220        230        240 
RNTFKVRSQI LSGIRQFMVN RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP 

       250        260        270        280        290        300 
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT 

       310        320        330        340        350        360 
LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIVESIGI 

       370        380        390        400        410        420 
HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 

       430        440        450        460        470        480 
REIGNGFSEL NDAEDQAQRF LDQVAAKDAG DDEAMFYDED YVTALEHGLP PTAGLGIGID 

       490        500 
RMVMLFTNSH TIRDVILFPA MRPVK 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58018.1.
BA000007 Genomic DNA. Translation: BAB37185.1.
PIRB91099.
F85944.
RefSeqNP_289459.1. NC_002655.2.
NP_311789.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8XD57.
SMRQ8XD57. Positions 12-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4228.

Proteomic databases

PRIDEQ8XD57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58018; AAG58018; Z4228.
BAB37185; BAB37185; BAB37185.
GeneID916412.
958385.
KEGGece:Z4228.
ecs:ECs3762.
PATRIC18357007. VBIEscCol44059_3682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1190.
HOGENOMHOG000236578.
KOK04567.
OMAGTEICLE.
OrthoDBEOG69PQ2M.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3729-MONOMER.
ECOO157:LYSS-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00252. Lys_tRNA_synth_class2.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR002313. Lys-tRNA-ligase_II.
IPR018149. Lys-tRNA-synth_II_C.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR00982. TRNASYNTHLYS.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00499. lysS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYK1_ECO57
AccessionPrimary (citable) accession number: Q8XD57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 86 of the entry and version 3 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