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Q6WRY5

- Q6WRY5_ENTFL

UniProt

Q6WRY5 - Q6WRY5_ENTFL

Protein

D-alanine--D-alanine ligase

Gene

vanG

Organism
Enterococcus faecalis (Streptococcus faecalis)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Cell wall formation.UniRule annotationSAAS annotation

    Catalytic activityi

    ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.UniRule annotationSAAS annotation

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei140 – 1401ADPImported
    Binding sitei190 – 1901ADPImported
    Binding sitei226 – 2261ADPImported
    Binding sitei261 – 2611ADPImported
    Metal bindingi299 – 2991Magnesium or manganese 1UniRule annotation
    Binding sitei301 – 3011ADPImported
    Metal bindingi312 – 3121Magnesium or manganese 1UniRule annotation
    Metal bindingi312 – 3121Magnesium or manganese 2UniRule annotation
    Metal bindingi314 – 3141Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 22856ATPUniRule annotationAdd
    BLAST
    Nucleotide bindingi181 – 1833ADPImported
    Nucleotide bindingi219 – 2224ADPImported
    Nucleotide bindingi311 – 3122ADPImported

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. D-alanine-D-alanine ligase activity Source: UniProtKB-HAMAP
    3. magnesium ion binding Source: UniProtKB-HAMAP
    4. manganese ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
    2. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    LigaseUniRule annotationSAAS annotationImported

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradationUniRule annotationSAAS annotation, Peptidoglycan synthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, ManganeseUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15480.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-alanine--D-alanine ligaseUniRule annotation (EC:6.3.2.4UniRule annotation)
    Alternative name(s):
    D-Ala-D-Ala ligaseUniRule annotation
    D-alanylalanine synthetaseUniRule annotation
    Gene namesi
    Name:vanGImported
    Synonyms:ddlUniRule annotation
    OrganismiEnterococcus faecalis (Streptococcus faecalis)Imported
    Taxonomic identifieri1351 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FU0X-ray2.35A/B1-349[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini144 – 345202ATP-graspUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the D-alanine--D-alanine ligase family.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation
    Contains ATP-grasp domain.SAAS annotation

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 2 hits.
    3.40.50.20. 1 hit.
    HAMAPiMF_00047. Dala_Dala_lig.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR000291. D-Ala_lig_Van_CS.
    IPR005905. D_ala_D_ala.
    IPR011095. Dala_Dala_lig_C.
    IPR011127. Dala_Dala_lig_N.
    IPR016185. PreATP-grasp_dom.
    [Graphical view]
    PANTHERiPTHR23132. PTHR23132. 1 hit.
    PfamiPF07478. Dala_Dala_lig_C. 1 hit.
    PF01820. Dala_Dala_lig_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01205. D_ala_D_alaTIGR. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS00843. DALA_DALA_LIGASE_1. 1 hit.
    PS00844. DALA_DALA_LIGASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6WRY5-1 [UniParc]FASTAAdd to Basket

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    MQNKKIAVIF GGNSTEYEVS LQSASAVFEN INTNKFDIIP IGITRSGEWY    50
    HYTGEKEKIL NNTWFEDSKN LCPVVVSQNR SVKGFLEIAS DKYRIIKVDL 100
    VFPVLHGKNG EDGTLQGIFE LAGIPVVGCD TLSSALCMDK DRAHKLVSLA 150
    GISVPKSVTF KRFNEEAAMK EIEANLTYPL FIKPVRAGSS FGITKVIEKQ 200
    ELDAAIELAF EHDTEVIVEE TINGFEVGCA VLGIDELIVG RVDEIELSSG 250
    FFDYTEKYTL KSSKIYMPAR IDAEAEKRIQ EAAVTIYKAL GCSGFSRVDM 300
    FYTPSGEIVF NEVNTIPGFT SHSRYPNMMK GIGLSFSQML DKLIGLYVE 349
    Length:349
    Mass (Da):38,730
    Last modified:July 5, 2004 - v1
    Checksum:i458EABDDF90493FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY271782 Genomic DNA. Translation: AAQ16273.1.
    DQ212986 Genomic DNA. Translation: ABA71731.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY271782 Genomic DNA. Translation: AAQ16273.1 .
    DQ212986 Genomic DNA. Translation: ABA71731.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FU0 X-ray 2.35 A/B 1-349 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci MetaCyc:MONOMER-15480.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 2 hits.
    3.40.50.20. 1 hit.
    HAMAPi MF_00047. Dala_Dala_lig.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR000291. D-Ala_lig_Van_CS.
    IPR005905. D_ala_D_ala.
    IPR011095. Dala_Dala_lig_C.
    IPR011127. Dala_Dala_lig_N.
    IPR016185. PreATP-grasp_dom.
    [Graphical view ]
    PANTHERi PTHR23132. PTHR23132. 1 hit.
    Pfami PF07478. Dala_Dala_lig_C. 1 hit.
    PF01820. Dala_Dala_lig_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01205. D_ala_D_alaTIGR. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS00843. DALA_DALA_LIGASE_1. 1 hit.
    PS00844. DALA_DALA_LIGASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The vanG glycopeptide resistance operon from Enterococcus faecalis revisited."
      Depardieu F., Bonora M.G., Reynolds P.E., Courvalin P.
      Mol. Microbiol. 50:931-948(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BM4518Imported.
    2. "VanG-type vancomycin-resistant Enterococcus faecalis strains isolated in Canada."
      Boyd D.A., Du T., Hizon R., Kaplen B., Murphy T., Tyler S., Brown S., Jamieson F., Weiss K., Mulvey M.R.
      Antimicrob. Agents Chemother. 50:2217-2221(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: G1-01247Imported.
    3. "Structural and functional characterization of VanG D-Ala:D-Ser ligase associated with vancomycin resistance in Enterococcus faecalis."
      Meziane-Cherif D., Saul F.A., Haouz A., Courvalin P.
      J. Biol. Chem. 287:37583-37592(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiQ6WRY5_ENTFL
    AccessioniPrimary (citable) accession number: Q6WRY5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3