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Protein

Diacylglycerol kinase

Gene

dagK

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. This ion appears to have a structural role and is required for catalytic activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41ATP1
Binding sitei94ATP1
Metal bindingi213Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi216Magnesium1 Publication1
Metal bindingi218Magnesium; via carbonyl oxygen1 Publication1
Active sitei273Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 14ATP5
Nucleotide bindingi67 – 73ATP7

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.1.107. 3352.

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
Ordered Locus Names:SAR1989
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68D → A: Loss of activity. 1 Publication1
Mutagenesisi91P → A: Loss of activity. 1 Publication1
Mutagenesisi94T → A: Loss of activity. 1 Publication1
Mutagenesisi96N → A: Loss of activity. 1 Publication1
Mutagenesisi97D → A: Loss of activity. 1 Publication1
Mutagenesisi124D → A: Loss of activity. 1 Publication1
Mutagenesisi168E → A: No effect on activity. 1 Publication1
Mutagenesisi216D → A: 5-fold decrease in activity. 1 Publication1
Mutagenesisi271D → A: Loss of activity. 1 Publication1
Mutagenesisi273E → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003864951 – 315Diacylglycerol kinaseAdd BLAST315

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-46022N.

Structurei

Secondary structure

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi18 – 31Combined sources14
Beta strandi34 – 40Combined sources7
Helixi46 – 54Combined sources9
Turni55 – 58Combined sources4
Beta strandi60 – 66Combined sources7
Helixi68 – 78Combined sources11
Beta strandi86 – 91Combined sources6
Helixi97 – 101Combined sources5
Helixi108 – 117Combined sources10
Beta strandi120 – 128Combined sources9
Beta strandi131 – 140Combined sources10
Helixi159 – 161Combined sources3
Turni166 – 169Combined sources4
Helixi170 – 172Combined sources3
Beta strandi176 – 182Combined sources7
Beta strandi185 – 199Combined sources15
Beta strandi214 – 217Combined sources4
Beta strandi219 – 225Combined sources7
Helixi229 – 239Combined sources11
Turni240 – 242Combined sources3
Helixi244 – 246Combined sources3
Beta strandi250 – 261Combined sources12
Beta strandi267 – 270Combined sources4
Beta strandi273 – 278Combined sources6
Beta strandi280 – 292Combined sources13
Beta strandi295 – 297Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QV7X-ray2.30A1-315[»]
2QVLX-ray2.40A1-315[»]
ProteinModelPortaliQ6GFF9.
SMRiQ6GFF9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GFF9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 132DAGKcPROSITE-ProRule annotationAdd BLAST132

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000261395.
KOiK07029.
OMAiEHINDPH.

Family and domain databases

Gene3Di3.40.50.10330. 1 hit.
InterProiIPR017438. ATP-NAD_kinase_dom_1.
IPR005218. Diacylglycerol/lipid_kinase.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
[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.

Q6GFF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRARIIYN PTSGKEQFKR ELPDALIKLE KAGYETSAYA TEKIGDATLE
60 70 80 90 100
AERAMHENYD VLIAAGGDGT LNEVVNGIAE KPNRPKLGVI PMGTVNDFGR
110 120 130 140 150
ALHIPNDIMG ALDVIIEGHS TKVDIGKMNN RYFINLAAGG QLTQVSYETP
160 170 180 190 200
SKLKSIVGPF AYYIKGFEML PQMKAVDLRI EYDGNVFQGE ALLFFLGLTN
210 220 230 240 250
SMAGFEKLVP DAKLDDGYFT LIIVEKSNLA ELGHIMTLAS RGEHTKHPKV
260 270 280 290 300
IYEKAKAINI SSFTDLQLNV DGEYGGKLPA NFLNLERHID VFAPNDIVNE
310
ELINNDHVDD NLIEE
Length:315
Mass (Da):34,902
Last modified:July 19, 2004 - v1
Checksum:i5EA85BFC769E1D0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40975.1.
RefSeqiWP_001231458.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG40975; CAG40975; SAR1989.
KEGGisar:SAR1989.
PATRICi19547619. VBIStaAur71814_2000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40975.1.
RefSeqiWP_001231458.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QV7X-ray2.30A1-315[»]
2QVLX-ray2.40A1-315[»]
ProteinModelPortaliQ6GFF9.
SMRiQ6GFF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46022N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG40975; CAG40975; SAR1989.
KEGGisar:SAR1989.
PATRICi19547619. VBIStaAur71814_2000.

Phylogenomic databases

HOGENOMiHOG000261395.
KOiK07029.
OMAiEHINDPH.

Enzyme and pathway databases

BRENDAi2.7.1.107. 3352.

Miscellaneous databases

EvolutionaryTraceiQ6GFF9.

Family and domain databases

Gene3Di3.40.50.10330. 1 hit.
InterProiIPR017438. ATP-NAD_kinase_dom_1.
IPR005218. Diacylglycerol/lipid_kinase.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
[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...

Entry informationi

Entry nameiDAGK_STAAR
AccessioniPrimary (citable) accession number: Q6GFF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 13, 2009
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 75 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.