Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A8N3

- SYK1_ECOLI

UniProt

P0A8N3 - SYK1_ECOLI

Protein

Lysine--tRNA ligase

Gene

lysS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi415 – 4151Magnesium 1By similarity
    Metal bindingi422 – 4221Magnesium 1By similarity
    Metal bindingi422 – 4221Magnesium 2By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. ligase activity Source: EcoliWiki
    3. lysine-tRNA ligase activity Source: EcoliWiki
    4. magnesium ion binding Source: UniProtKB-HAMAP
    5. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. lysyl-tRNA aminoacylation Source: EcoliWiki
    2. tRNA aminoacylation for protein translation Source: EcoliWiki

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine--tRNA ligase (EC:6.1.1.6)
    Alternative name(s):
    Lysyl-tRNA synthetase
    Short name:
    LysRS
    Gene namesi
    Name:lysS
    Synonyms:asuD, herC
    Ordered Locus Names:b2890, JW2858
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10552. lysS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 505504Lysine--tRNA ligasePRO_0000152622Add
    BLAST

    Proteomic databases

    PaxDbiP0A8N3.
    PRIDEiP0A8N3.

    2D gel databases

    SWISS-2DPAGEP0A8N3.

    PTM databases

    PhosSiteiP0809407.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A8N3.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-36211N.
    IntActiP0A8N3. 24 interactions.
    MINTiMINT-1227180.
    STRINGi511145.b2890.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3219
    Helixi46 – 538
    Helixi58 – 647
    Beta strandi67 – 7913
    Beta strandi81 – 9010
    Beta strandi93 – 1008
    Turni101 – 1033
    Helixi108 – 1114
    Helixi113 – 1153
    Beta strandi118 – 1203
    Beta strandi121 – 13010
    Beta strandi131 – 1355
    Beta strandi136 – 14712
    Helixi165 – 1684
    Helixi170 – 1767
    Helixi178 – 19922
    Turni200 – 2023
    Beta strandi210 – 2145
    Beta strandi224 – 2274
    Turni228 – 2314
    Beta strandi232 – 2365
    Helixi241 – 2499
    Beta strandi254 – 2629
    Beta strandi273 – 28412
    Helixi287 – 30620
    Beta strandi309 – 3135
    Beta strandi316 – 3227
    Beta strandi325 – 3284
    Helixi329 – 3368
    Helixi342 – 3465
    Helixi348 – 35710
    Helixi368 – 38013
    Helixi381 – 3833
    Beta strandi386 – 3949
    Helixi395 – 3973
    Beta strandi399 – 4013
    Beta strandi410 – 4189
    Beta strandi421 – 4299
    Helixi433 – 44816
    Helixi459 – 4668
    Beta strandi471 – 4788
    Helixi479 – 4879
    Helixi492 – 4943
    Beta strandi496 – 4983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BBUX-ray2.70A2-505[»]
    1BBWX-ray2.70A2-505[»]
    1KRSNMR-A31-149[»]
    1KRTNMR-A31-149[»]
    ProteinModelPortaliP0A8N3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8N3.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1190.
    HOGENOMiHOG000236578.
    KOiK04567.
    OMAiGTEICLE.
    OrthoDBiEOG69PQ2M.
    PhylomeDBiP0A8N3.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_00252. Lys_tRNA_synth_class2.
    InterProiIPR004364. 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]
    PANTHERiPTHR22594. PTHR22594. 1 hit.
    PfamiPF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    PRINTSiPR00982. TRNASYNTHLYS.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A8N3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH    50
    AEFDGKENEE LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA 100
    RDDLPEGVYN EQFKKWDLGD ILGAKGKLFK TKTGELSIHC TELRLLTKAL 150
    RPLPDKFHGL QDQEARYRQR YLDLISNDES RNTFKVRSQI LSGIRQFMVN 200
    RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP ELYLKRLVVG 250
    GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT 300
    LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS 350
    AKAIAESIGI HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL 400
    ARRNDVNPEI TDRFEFFIGG REIGNGFSEL NDAEDQAQRF LDQVAAKDAG 450
    DDEAMFYDED YVTALEHGLP PTAGLGIGID RMVMLFTNSH TIRDVILFPA 500
    MRPVK 505
    Length:505
    Mass (Da):57,603
    Last modified:January 23, 2007 - v2
    Checksum:iF2CA901FBA63CFEF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03795 Genomic DNA. Translation: AAA23959.1.
    U28375 Genomic DNA. Translation: AAA83071.1.
    U00096 Genomic DNA. Translation: AAC75928.1.
    AP009048 Genomic DNA. Translation: BAE76955.1.
    PIRiB65073. SYECKT.
    RefSeqiNP_417366.1. NC_000913.3.
    YP_491091.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75928; AAC75928; b2890.
    BAE76955; BAE76955; BAE76955.
    GeneIDi12933343.
    947372.
    KEGGiecj:Y75_p2822.
    eco:b2890.
    PATRICi32121190. VBIEscCol129921_2983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03795 Genomic DNA. Translation: AAA23959.1 .
    U28375 Genomic DNA. Translation: AAA83071.1 .
    U00096 Genomic DNA. Translation: AAC75928.1 .
    AP009048 Genomic DNA. Translation: BAE76955.1 .
    PIRi B65073. SYECKT.
    RefSeqi NP_417366.1. NC_000913.3.
    YP_491091.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BBU X-ray 2.70 A 2-505 [» ]
    1BBW X-ray 2.70 A 2-505 [» ]
    1KRS NMR - A 31-149 [» ]
    1KRT NMR - A 31-149 [» ]
    ProteinModelPortali P0A8N3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36211N.
    IntActi P0A8N3. 24 interactions.
    MINTi MINT-1227180.
    STRINGi 511145.b2890.

    PTM databases

    PhosSitei P0809407.

    2D gel databases

    SWISS-2DPAGE P0A8N3.

    Proteomic databases

    PaxDbi P0A8N3.
    PRIDEi P0A8N3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75928 ; AAC75928 ; b2890 .
    BAE76955 ; BAE76955 ; BAE76955 .
    GeneIDi 12933343.
    947372.
    KEGGi ecj:Y75_p2822.
    eco:b2890.
    PATRICi 32121190. VBIEscCol129921_2983.

    Organism-specific databases

    EchoBASEi EB0547.
    EcoGenei EG10552. lysS.

    Phylogenomic databases

    eggNOGi COG1190.
    HOGENOMi HOG000236578.
    KOi K04567.
    OMAi GTEICLE.
    OrthoDBi EOG69PQ2M.
    PhylomeDBi P0A8N3.

    Enzyme and pathway databases

    BioCyci EcoCyc:LYSS-MONOMER.
    ECOL316407:JW2858-MONOMER.
    MetaCyc:LYSS-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A8N3.
    PROi P0A8N3.

    Gene expression databases

    Genevestigatori P0A8N3.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_00252. Lys_tRNA_synth_class2.
    InterProi IPR004364. 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 ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    Pfami PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PRINTSi PR00982. TRNASYNTHLYS.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00499. lysS_bact. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiSYK1_ECOLI
    AccessioniPrimary (citable) accession number: P0A8N3
    Secondary accession number(s): P13030, Q2M9V1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3