ID   DAGK_STAAW              Reviewed;         315 AA.
AC   Q7A0H3;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Diacylglycerol kinase;
DE            Short=DAG kinase;
DE            Short=DAGK;
DE            EC=2.7.1.107 {ECO:0000250|UniProtKB:Q6GFF9};
GN   Name=dagK; OrderedLocusNames=MW1839;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of diacylglycerol (DAG) into
CC       phosphatidic acid. Is a key enzyme involved in the production of
CC       lipoteichoic acid by reintroducing DAG formed from the breakdown of
CC       membrane phospholipids into the phosphatidylglycerol biosynthetic
CC       pathway. {ECO:0000250|UniProtKB:Q6GFF9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC         ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000250|UniProtKB:Q6GFF9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q6GFF9};
CC       Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC       structural role and is required for catalytic activity.
CC       {ECO:0000250|UniProtKB:Q6GFF9};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6GFF9}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB95704.1; -; Genomic_DNA.
DR   RefSeq; WP_001231451.1; NC_003923.1.
DR   AlphaFoldDB; Q7A0H3; -.
DR   SMR; Q7A0H3; -.
DR   EnsemblBacteria; BAB95704; BAB95704; BAB95704.
DR   KEGG; sam:MW1839; -.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   OMA; GFDSRVN; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   TIGRFAMs; TIGR00147; TIGR00147; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..315
FT                   /note="Diacylglycerol kinase"
FT                   /id="PRO_0000386498"
FT   DOMAIN          1..132
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT   BINDING         10..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         67..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GFF9"
SQ   SEQUENCE   315 AA;  34887 MW;  C5CC706B5E3A0F00 CRC64;
     MRKRARIIYN PTSGKELFKR ELPDALIKLE KAGYETSAYA TEKIGDATLE AERAMHENYD
     VLIAAGGDGT LNEVVNGIAE KPNRPKLGVI PMGTVNDFGR ALHIPNDIMG ALDVIIEGHS
     TKVDIGKMNN RYFINLAAGG QLTQVSYETP SKLKSIVGPF AYYIKGFEML PQMKAVDLRI
     EYDGNVFQGE ALLFFLGLTN SMAGFEKLVP DAKLDDGYFT LIIVEKSNLA ELGHIMTLAS
     RGEHTKHPKV IYEKAKAINI SSFTDLQLNV DGEYGGKLPA NFLNLERHID VFAPNDIVNE
     ELINNDHVDD NLIEE