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O31502

- DAGK_BACSU

UniProt

O31502 - DAGK_BACSU

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Protein
Diacylglycerol kinase
Gene
dagK, dgkB, yerQ, BSU06720
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Binds 1 magnesium 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 – 401ATP By similarity
Binding sitei93 – 931ATP By similarity
Metal bindingi213 – 2131Magnesium; via carbonyl oxygen By similarity
Metal bindingi216 – 2161Magnesium By similarity
Metal bindingi218 – 2181Magnesium; via carbonyl oxygen By similarity
Active sitei273 – 2731Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 135ATP By similarity
Nucleotide bindingi66 – 727ATP By similarity

GO - Molecular functioni

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

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: 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 kinase
PRO_0000386482Add
BLAST

Proteomic databases

PaxDbiO31502.

Interactioni

Protein-protein interaction databases

IntActiO31502. 2 interactions.
STRINGi224308.BSU06720.

Structurei

3D structure databases

ProteinModelPortaliO31502.
SMRiO31502. Positions 1-301.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 132132DAGKc
Add
BLAST

Sequence similaritiesi

Contains 1 DAGKc domain.

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

« 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(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: July 9, 2014
This is version 82 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

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