DAGK_STAAM
ID DAGK_STAAM Reviewed; 315 AA.
AC Q99SY8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SAV1898;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB58060.1; -; Genomic_DNA.
DR RefSeq; WP_001231451.1; NC_002758.2.
DR AlphaFoldDB; Q99SY8; -.
DR SMR; Q99SY8; -.
DR PaxDb; Q99SY8; -.
DR EnsemblBacteria; BAB58060; BAB58060; SAV1898.
DR KEGG; sav:SAV1898; -.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OMA; GFDSRVN; -.
DR PhylomeDB; Q99SY8; -.
DR BioCyc; SAUR158878:SAV_RS10395-MON; -.
DR Proteomes; UP000002481; 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_0000386493"
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
