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)

O31502

- DAGK_BACSU

UniProt

O31502 - DAGK_BACSU

Protein

Diacylglycerol kinase

Gene

dagK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine.1 Publication

    Catalytic activityi

    ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.1 Publication

    Cofactori

    Binds 1 magnesium ion per subunit. This ion appears to have a structural role and is required for catalytic activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401ATPPROSITE-ProRule annotation
    Binding sitei93 – 931ATPPROSITE-ProRule annotation
    Metal bindingi213 – 2131Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi216 – 2161MagnesiumBy similarity
    Metal bindingi218 – 2181Magnesium; via carbonyl oxygenBy similarity
    Active sitei273 – 2731Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 135ATPPROSITE-ProRule annotation
    Nucleotide bindingi66 – 727ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. diacylglycerol kinase activity Source: CACAO
    3. metal ion binding Source: UniProtKB-KW
    4. NAD+ kinase activity Source: InterPro

    GO - Biological processi

    1. phospholipid biosynthetic process Source: UniProtKB-KW
    2. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciBSUB:BSU06720-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diacylglycerol kinase (EC:2.7.1.107)
    Short name:
    DAG kinase
    Short name:
    DAGK
    Gene namesi
    Name:dagK
    Synonyms:dgkB, yerQ
    Ordered Locus Names:BSU06720
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU06720. [Micado]

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are not viable. They exhibit accumulation of diacylglycerol, disappearance of phosphatidylglycerol, and the cessation of lipoteichoic acid formation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 303303Diacylglycerol kinasePRO_0000386482Add
    BLAST

    Proteomic databases

    PaxDbiO31502.

    Interactioni

    Protein-protein interaction databases

    IntActiO31502. 2 interactions.
    STRINGi224308.BSU06720.

    Structurei

    3D structure databases

    ProteinModelPortaliO31502.
    SMRiO31502. Positions 1-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 132132DAGKcPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the diacylglycerol/lipid kinase family.Curated
    Contains 1 DAGKc domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1597.
    HOGENOMiHOG000261395.
    KOiK07029.
    OMAiYLKGMEM.
    OrthoDBiEOG613098.
    PhylomeDBiO31502.

    Family and domain databases

    Gene3Di3.40.50.10330. 1 hit.
    InterProiIPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR005218. Diacylglycerol/lipid_kinase.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [Graphical view]
    PfamiPF00781. DAGK_cat. 1 hit.
    [Graphical view]
    SMARTiSM00046. DAGKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 1 hit.
    TIGRFAMsiTIGR00147. TIGR00147. 1 hit.
    PROSITEiPS50146. DAGK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O31502-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRARIIYNP TSGREIFKKH LAQVLQKFEQ AGYETSTHAT TCAGDATHAA    50
    KEAALREFDL IIAAGGDGTI NEVVNGLAPL DNRPTLGVIP VGTTNDFARA 100
    LGIPREDILK AADTVINGVA RPIDIGQVNG QYFINIAGGG RLTELTYDVP 150
    SKLKTMLGQL AYYLKGMEML PSLRPTEVEI EYDGKLFQGE IMLFLVTLTN 200
    SVGGFEKLAP DSSLNDGMFD LMILKKANLA EFIRVATMAL RGEHINDQHI 250
    IYTKANRVKV NVSEKMQLNL DGEYGGMLPG EFVNLYRHIH VVMPKEKAEQ 300
    LDD 303
    Length:303
    Mass (Da):33,337
    Last modified:January 1, 1998 - v1
    Checksum:i533F3658A41A5998
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB12492.1.
    PIRiF69795.
    RefSeqiNP_388554.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12492; CAB12492; BSU06720.
    GeneIDi936061.
    KEGGibsu:BSU06720.
    PATRICi18972990. VBIBacSub10457_0709.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB12492.1 .
    PIRi F69795.
    RefSeqi NP_388554.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O31502.
    SMRi O31502. Positions 1-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O31502. 2 interactions.
    STRINGi 224308.BSU06720.

    Proteomic databases

    PaxDbi O31502.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12492 ; CAB12492 ; BSU06720 .
    GeneIDi 936061.
    KEGGi bsu:BSU06720.
    PATRICi 18972990. VBIBacSub10457_0709.

    Organism-specific databases

    GenoListi BSU06720. [Micado ]

    Phylogenomic databases

    eggNOGi COG1597.
    HOGENOMi HOG000261395.
    KOi K07029.
    OMAi YLKGMEM.
    OrthoDBi EOG613098.
    PhylomeDBi O31502.

    Enzyme and pathway databases

    BioCyci BSUB:BSU06720-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.10330. 1 hit.
    InterProi IPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR005218. Diacylglycerol/lipid_kinase.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00781. DAGK_cat. 1 hit.
    [Graphical view ]
    SMARTi SM00046. DAGKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 1 hit.
    TIGRFAMsi TIGR00147. TIGR00147. 1 hit.
    PROSITEi PS50146. DAGK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis."
      Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.
      J. Biol. Chem. 282:21738-21745(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DIACYLGLYCEROL KINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiDAGK_BACSU
    AccessioniPrimary (citable) accession number: O31502
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 13, 2009
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 83 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, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3