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)

Q0TEI8

- LUXS_ECOL5

UniProt

Q0TEI8 - LUXS_ECOL5

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).UniRule annotation

    Catalytic activityi

    S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.UniRule annotation

    Cofactori

    Binds 1 iron ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541IronUniRule annotation
    Metal bindingi58 – 581IronUniRule annotation
    Metal bindingi128 – 1281IronUniRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. quorum sensing Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Autoinducer synthesis, Quorum sensing

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciECOL362663:GIY5-2669-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-ribosylhomocysteine lyaseUniRule annotation (EC:4.4.1.21UniRule annotation)
    Alternative name(s):
    AI-2 synthesis proteinUniRule annotation
    Autoinducer-2 production protein LuxSUniRule annotation
    Gene namesi
    Name:luxSUniRule annotation
    Ordered Locus Names:ECP_2652
    OrganismiEscherichia coli O6:K15:H31 (strain 536 / UPEC)
    Taxonomic identifieri362663 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000009182: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 171171S-ribosylhomocysteine lyasePRO_0000297997Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi362663.ECP_2652.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0TEI8.
    SMRiQ0TEI8. Positions 3-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LuxS family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1854.
    HOGENOMiHOG000040371.
    KOiK07173.
    OMAiRDHLNSD.
    OrthoDBiEOG68WRBM.

    Family and domain databases

    Gene3Di3.30.1360.80. 1 hit.
    HAMAPiMF_00091. LuxS.
    InterProiIPR011249. Metalloenz_LuxS/M16.
    IPR003815. S-ribosylhomocysteinase.
    [Graphical view]
    PfamiPF02664. LuxS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006160. AI2. 1 hit.
    PRINTSiPR01487. LUXSPROTEIN.
    ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF63411. SSF63411. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q0TEI8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE    50
    RGIHTLEHLF AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV 100
    ADAWKAAMED VLKVQDQNQI PELNVYQCGT YQMHSLQEAQ DIARNILERD 150
    VRINSNEELA LPKEKLQELH I 171
    Length:171
    Mass (Da):19,443
    Last modified:September 5, 2006 - v1
    Checksum:i131F4B204B6DA105
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000247 Genomic DNA. Translation: ABG70641.1.
    RefSeqiYP_670542.1. NC_008253.1.

    Genome annotation databases

    EnsemblBacteriaiABG70641; ABG70641; ECP_2652.
    GeneIDi4190722.
    KEGGiecp:ECP_2652.
    PATRICi18196117. VBIEscCol77757_2691.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000247 Genomic DNA. Translation: ABG70641.1 .
    RefSeqi YP_670542.1. NC_008253.1.

    3D structure databases

    ProteinModelPortali Q0TEI8.
    SMRi Q0TEI8. Positions 3-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 362663.ECP_2652.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG70641 ; ABG70641 ; ECP_2652 .
    GeneIDi 4190722.
    KEGGi ecp:ECP_2652.
    PATRICi 18196117. VBIEscCol77757_2691.

    Phylogenomic databases

    eggNOGi COG1854.
    HOGENOMi HOG000040371.
    KOi K07173.
    OMAi RDHLNSD.
    OrthoDBi EOG68WRBM.

    Enzyme and pathway databases

    BioCyci ECOL362663:GIY5-2669-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1360.80. 1 hit.
    HAMAPi MF_00091. LuxS.
    InterProi IPR011249. Metalloenz_LuxS/M16.
    IPR003815. S-ribosylhomocysteinase.
    [Graphical view ]
    Pfami PF02664. LuxS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006160. AI2. 1 hit.
    PRINTSi PR01487. LUXSPROTEIN.
    ProDomi PD013172. S-ribosylhomocysteinase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF63411. SSF63411. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
      Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
      Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 536 / UPEC.

    Entry informationi

    Entry nameiLUXS_ECOL5
    AccessioniPrimary (citable) accession number: Q0TEI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3