DAGK_STAHJ
ID DAGK_STAHJ Reviewed; 330 AA.
AC Q4L7L1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SH1055;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04364.1; -; Genomic_DNA.
DR RefSeq; WP_011275360.1; NC_007168.1.
DR AlphaFoldDB; Q4L7L1; -.
DR SMR; Q4L7L1; -.
DR STRING; 279808.SH1055; -.
DR EnsemblBacteria; BAE04364; BAE04364; SH1055.
DR GeneID; 58062770; -.
DR KEGG; sha:SH1055; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OMA; GFDSRVN; -.
DR OrthoDB; 869726at2; -.
DR Proteomes; UP000000543; 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..330
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000386502"
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"
SQ SEQUENCE 330 AA; 36803 MW; 218DD852D68697D1 CRC64;
MRKCARIIYN PTSGKELFKR TLPDVLIKLE RAGYETSAYA TEREGDATLE AERALKRDYD
IIIAAGGDGT LNEVVNGIAE QPNRPKLGII PMGTVNDFGR ALHLPSDIMG AVDVIIDDHT
TKVDIGKMNN RYFINLAAGG QLTQVSYETP SRLKSIVGPF AYYIKGFEML PQMKAVDLRI
EYDNQVFQGE ALLFLLGLTN SMAGFEKLVP DAKLDDGHFT LIIVEKANLA ELGHIMTLAS
RGEHIKHPKV IYEKAKSINI SSFTEMQLNV DGEYGGKLPA NFLNLKRHIE VCTPKDIYNE
ELTEDQQVED GIIEEKPSNE EIIKNNEISE
