ID   Y736_STAA8              Reviewed;         305 AA.
AC   Q2G084;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Putative lipid kinase SAOUHSC_00736;
DE            EC=2.7.1.-;
GN   OrderedLocusNames=SAOUHSC_00736;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids
CC       other than diacylglycerol (DAG). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC       structural role and is required for catalytic activity. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD29869.1; -; Genomic_DNA.
DR   RefSeq; WP_000429014.1; NZ_LS483365.1.
DR   RefSeq; YP_499296.1; NC_007795.1.
DR   AlphaFoldDB; Q2G084; -.
DR   SMR; Q2G084; -.
DR   STRING; 1280.SAXN108_0794; -.
DR   EnsemblBacteria; ABD29869; ABD29869; SAOUHSC_00736.
DR   GeneID; 3920981; -.
DR   KEGG; sao:SAOUHSC_00736; -.
DR   PATRIC; fig|93061.5.peg.666; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   OMA; LPGGTCN; -.
DR   PRO; PR:Q2G084; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="Putative lipid kinase SAOUHSC_00736"
FT                   /id="PRO_0000386508"
FT   DOMAIN          3..139
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         74..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33626 MW;  9D195C905AA651E1 CRC64;
     MENKYTHGVL FYHEHSGLKN INQGIGEVTT ALSSICKHLS IQLSENEGDI IKYCQEIKTK
     NYAKDVDILF ILGGDGTVNE LINGVMTHDL QLPIGILPGG TFNDFTKTLN IAPNHKQASE
     QMISAQVGTY DVIKINNQYA LNFVGLGLIV QNAENVQDGS KDIFGKLSYI GSTVKTLLNP
     TQFNYQLSID DKTYSGETTM ILTANGPFIG GSRIPLTDLS PQDGELNTFI FNEQSFSILN
     DIFKKRDSMN WNEITQGIEH IPGKKISLTT DPAMKVDIDG EISLETPIDI EVIPNAIQLL
     TVNDL