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Protein

Diacylglycerol kinase

Gene

dagK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit. This ion appears to have a structural role and is required for catalytic activity.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
Complete GO annotation...

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 Componenti: 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.
InParanoidiO31502.
KOiK07029.
OMAiRGEHIND.
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

        10         20         30         40         50
MKRARIIYNP TSGREIFKKH LAQVLQKFEQ AGYETSTHAT TCAGDATHAA
60 70 80 90 100
KEAALREFDL IIAAGGDGTI NEVVNGLAPL DNRPTLGVIP VGTTNDFARA
110 120 130 140 150
LGIPREDILK AADTVINGVA RPIDIGQVNG QYFINIAGGG RLTELTYDVP
160 170 180 190 200
SKLKTMLGQL AYYLKGMEML PSLRPTEVEI EYDGKLFQGE IMLFLVTLTN
210 220 230 240 250
SVGGFEKLAP DSSLNDGMFD LMILKKANLA EFIRVATMAL RGEHINDQHI
260 270 280 290 300
IYTKANRVKV NVSEKMQLNL DGEYGGMLPG EFVNLYRHIH VVMPKEKAEQ

LDD
Length:303
Mass (Da):33,337
Last modified:January 1, 1998 - v1
Checksum:i533F3658A41A5998
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12492.1.
PIRiF69795.
RefSeqiNP_388554.1. NC_000964.3.

3D structure databases

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

Protein-protein interaction databases

IntActiO31502. 2 interactions.
STRINGi224308.BSU06720.

Proteomic databases

PaxDbiO31502.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU06720. [Micado]

Phylogenomic databases

eggNOGiCOG1597.
HOGENOMiHOG000261395.
InParanoidiO31502.
KOiK07029.
OMAiRGEHIND.
OrthoDBiEOG613098.
PhylomeDBiO31502.

Enzyme and pathway databases

BioCyciBSUB:BSU06720-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(2006) [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: January 7, 2015
This is version 86 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.