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P0A8N3 (SYK1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:asuD, herC
Ordered Locus Names:b2890, JW2858
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm HAMAP-Rule MF_00252.

Miscellaneous

There are two lysyl-tRNA ligases in E.coli: lysS is expressed constitutively, while lysU is heat inducible.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 505504Lysine--tRNA ligase HAMAP-Rule MF_00252
PRO_0000152622

Sites

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

Secondary structure

.............................................................................. 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8N3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F2CA901FBA63CFEF

FASTA50557,603
        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 AKAIAESIGI 

       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

« Hide 'large scale' references
[1]"Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli."
Kawakami K., Joensson Y.H., Bjoerk G.R., Ikeda H., Nakamura Y.
Proc. Natl. Acad. Sci. U.S.A. 85:5620-5624(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species."
Leveque F., Plateau P., Dessen P., Blanquet S.
Nucleic Acids Res. 18:305-312(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[6]"Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys)."
Commans S., Plateau P., Blanquet S., Dardel F.
J. Mol. Biol. 253:100-113(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03795 Genomic DNA. Translation: AAA23959.1.
U28375 Genomic DNA. Translation: AAA83071.1.
U00096 Genomic DNA. Translation: AAC75928.1.
AP009048 Genomic DNA. Translation: BAE76955.1.
PIRSYECKT. B65073.
RefSeqNP_417366.1. NC_000913.3.
YP_491091.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBUX-ray2.70A2-504[»]
1BBWX-ray2.70A2-504[»]
1KRSNMR-A31-149[»]
1KRTNMR-A31-149[»]
ProteinModelPortalP0A8N3.
SMRP0A8N3. Positions 12-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36211N.
IntActP0A8N3. 24 interactions.
MINTMINT-1227180.
STRING511145.b2890.

PTM databases

PhosSiteP0809407.

2D gel databases

SWISS-2DPAGEP0A8N3.

Proteomic databases

PaxDbP0A8N3.
PRIDEP0A8N3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75928; AAC75928; b2890.
BAE76955; BAE76955; BAE76955.
GeneID12933343.
947372.
KEGGecj:Y75_p2822.
eco:b2890.
PATRIC32121190. VBIEscCol129921_2983.

Organism-specific databases

EchoBASEEB0547.
EcoGeneEG10552. lysS.

Phylogenomic databases

eggNOGCOG1190.
HOGENOMHOG000236578.
KOK04567.
OMAEINIHEA.
OrthoDBEOG69PQ2M.
PhylomeDBP0A8N3.
ProtClustDBPRK00484.

Enzyme and pathway databases

BioCycEcoCyc:LYSS-MONOMER.
ECOL316407:JW2858-MONOMER.
MetaCyc:LYSS-MONOMER.

Gene expression databases

GenevestigatorP0A8N3.

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.
PTHR22594:SF4. PTHR22594:SF4. 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...

Other

EvolutionaryTraceP0A8N3.
PROP0A8N3.

Entry information

Entry nameSYK1_ECOLI
AccessionPrimary (citable) accession number: P0A8N3
Secondary accession number(s): P13030, Q2M9V1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries