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)

Q0SND6

- LUXS_BORAP

UniProt

Q0SND6 - LUXS_BORAP

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Borrelia afzelii (strain PKo)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  1. 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 bindingi53 – 531IronUniRule annotation
    Metal bindingi57 – 571IronUniRule annotation
    Metal bindingi124 – 1241IronUniRule 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

    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:BAPKO_0386, BafPKo_0376
    OrganismiBorrelia afzelii (strain PKo)
    Taxonomic identifieri390236 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group
    ProteomesiUP000001825: Chromosome, UP000005216: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 157157S-ribosylhomocysteine lyasePRO_0000297986Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi390236.BAPKO_0386.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0SND6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LuxS family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1854.
    HOGENOMiHOG000040372.
    KOiK07173.
    OMAiDLISWLF.
    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.

    Q0SND6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKITSFTID HTKLNPGIYV SRKDTFENVI FTTIDIRIKA PNIEPIIENA    50
    AIHTIEHIGA TLLRNNEVWA EKIVYFGPMG CRTGFYLIIF GNYESKDLID 100
    LISWLFSEIV NFSEPIPGAS HKECGNYKEH NLDMAKYESS KYLQILNNIK 150
    EENLKYP 157
    Length:157
    Mass (Da):18,117
    Last modified:September 5, 2006 - v1
    Checksum:i93D93BE926FB3548
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000395 Genomic DNA. Translation: ABH01642.1.
    CP002933 Genomic DNA. Translation: AEL69602.1.
    RefSeqiYP_005592592.1. NC_017238.1.
    YP_709818.1. NC_008277.1.

    Genome annotation databases

    EnsemblBacteriaiABH01642; ABH01642; BAPKO_0386.
    AEL69602; AEL69602; BafPKo_0376.
    GeneIDi12159330.
    4227565.
    KEGGibaf:BAPKO_0386.
    bafz:BafPKo_0376.
    PATRICi37189056. VBIBorAfz3878_0440.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000395 Genomic DNA. Translation: ABH01642.1 .
    CP002933 Genomic DNA. Translation: AEL69602.1 .
    RefSeqi YP_005592592.1. NC_017238.1.
    YP_709818.1. NC_008277.1.

    3D structure databases

    ProteinModelPortali Q0SND6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 390236.BAPKO_0386.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABH01642 ; ABH01642 ; BAPKO_0386 .
    AEL69602 ; AEL69602 ; BafPKo_0376 .
    GeneIDi 12159330.
    4227565.
    KEGGi baf:BAPKO_0386.
    bafz:BafPKo_0376.
    PATRICi 37189056. VBIBorAfz3878_0440.

    Phylogenomic databases

    eggNOGi COG1854.
    HOGENOMi HOG000040372.
    KOi K07173.
    OMAi DLISWLF.
    OrthoDBi EOG68WRBM.

    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. "Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
      Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
      BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PKo.
    2. "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
      Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
      J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PKo.

    Entry informationi

    Entry nameiLUXS_BORAP
    AccessioniPrimary (citable) accession number: Q0SND6
    Secondary accession number(s): G0IS21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 56 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