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Reviewed, UniProtKB/Swiss-Prot P0A8N7 (SYK3_ECOLI)

Last modified June 16, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative lysyl-tRNA synthetase
    EC=6.1.1.6
Alternative name(s):
    Lysine--tRNA ligase
      Short name=LysRS
    GX
Gene names
Name: poxA
Synonyms: genX, yjeA
Ordered Locus Names: b4155, JW4116
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Could be a lysyl-tRNA synthetase. HAMAP MF_00174

Catalytic activity

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP MF_00174

Disruption phenotype

Cell have a reduced pyruvate oxidase activity and a reduced growth rate. Ref.6

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlysyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

lysine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceEP0AFG81EBI-562598,EBI-542683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Putative lysyl-tRNA synthetase HAMAP MF_00174
PRO_0000152719

Experimental info

Sequence conflict781E → Q in AAA23436. Ref.5
Sequence conflict1441A → E in AAA23436. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P0A8N7-1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: F72B535CCA23E4CC

FASTA32536,976
        10         20         30         40         50         60 
MSETASWQPS ASIPNLLKRA AIMAEIRRFF ADRGVLEVET PCMSQATVTD IHLVPFETRF 

        70         80         90        100        110        120 
VGPGHSQGMN LWLMTSPEYH MKRLLVAGCG PVFQLCRSFR NEEMGRYHNP EFTMLEWYRP 

       130        140        150        160        170        180 
HYDMYRLMNE VDDLLQQVLD CPAAESLSYQ QAFLRYLEID PLSADKTQLR EVAAKLDLSN 

       190        200        210        220        230        240 
VADTEEDRDT LLQLLFTFGV EPNIGKEKPT FVYHFPASQA SLAQISTEDH RVAERFEVYY 

       250        260        270        280        290        300 
KGIELANGFH ELTDAREQQQ RFEQDNRKRA ARGLPQHPID QNLIEALKVG MPDCSGVALG 

       310        320 
VDRLVMLALG AETLAEVIAF SVDRA 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for a new Escherichia coli protein resembling a lysyl-tRNA synthetase."
Kong L., Fromant M., Blanquet S., Plateau P.
Gene 108:163-164(1991) [PubMed: 1761227] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli."
Cole S.T.
Eur. J. Biochem. 122:479-484(1982) [PubMed: 7037404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
[6]"Mapping nonselectable genes of Escherichia coli by using transposon Tn10: location of a gene affecting pyruvate oxidase."
Chang Y.-Y., Cronan J.E. Jr.
J. Bacteriol. 151:1279-1289(1982) [PubMed: 6286595] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: K12.
[7]"Homology of aspartyl- and lysyl-tRNA synthetases."
Gampel A., Tzagoloff A.
Proc. Natl. Acad. Sci. U.S.A. 86:6023-6027(1989) [PubMed: 2668951] [Abstract]
Cited for: SIMILARITY TO CLASS-II AA-TRNA SYNTHETASES.

Cross-references

Sequence databases

X59988 Genomic DNA. Translation: CAA42604.1.
U14003 Genomic DNA. Translation: AAA97054.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77115.1.
AP009048 Genomic DNA. Translation: BAE78159.1.
J01611 Genomic DNA. Translation: AAA23436.2.
PIRS56383.
RefSeqAP_004658.1.
NP_418579.2.

3D structure databases

HSSPHSSP built from PDB template 1E1O based on UniProtKB P14825.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A8N7. 3 interactions.

Genome annotation databases

GeneID948672.
GenomeReviewsGene locus JW4116 in contig AP009048_GR.
Gene locus b4155 in contig U00096_GR.
KEGGecj:JW4116.
eco:b4155.

Organism-specific databases

EchoBASEEB1196.
EcoGeneEG11211. poxA.
CMRSearch...

Phylogenomic databases

HOGENOMP0A8N7.
OMAP0A8N7. VFRNEEA.

Enzyme and pathway databases

BioCycEcoCyc:EG11211-MON.

Family and domain databases

HAMAPMF_00174.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004525. Lys-tRNA-synth-rel.
IPR018149. Lys-tRNA-synth_II_C.
[Graphical view]
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
[Graphical view]
PRINTSPR00982. TRNASYNTHLYS.
TIGRFAMsTIGR00462. genX. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYK3_ECOLI
AccessionPrimary (citable) accession number: P0A8N7
Secondary accession number(s): P03812 expand/collapse secondary AC list , P78141, Q2M6E7, Q8XDP9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents