DAGK_BACSU
ID DAGK_BACSU Reviewed; 303 AA.
AC O31502;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Diacylglycerol kinase {ECO:0000303|PubMed:17535816};
DE Short=DAG kinase;
DE Short=DAGK;
DE EC=2.7.1.107 {ECO:0000269|PubMed:17535816};
GN Name=dagK; Synonyms=dgkB, yerQ; OrderedLocusNames=BSU06720;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION AS A DIACYLGLYCEROL KINASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17535816; DOI=10.1074/jbc.m703536200;
RA Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT "Identification of a soluble diacylglycerol kinase required for
RT lipoteichoic acid production in Bacillus subtilis.";
RL J. Biol. Chem. 282:21738-21745(2007).
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. Is more active toward long-chain DAG compared with short-chain
CC DAG. Is not able to phosphorylate substrates other than DAG, such as
CC monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or
CC sphingosine. {ECO:0000269|PubMed:17535816}.
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:0000269|PubMed:17535816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:17535816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17535816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000269|PubMed:17535816};
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not viable. They
CC exhibit accumulation of diacylglycerol, disappearance of
CC phosphatidylglycerol, and the cessation of lipoteichoic acid formation.
CC {ECO:0000269|PubMed:17535816}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB12492.1; -; Genomic_DNA.
DR PIR; F69795; F69795.
DR RefSeq; NP_388554.1; NC_000964.3.
DR RefSeq; WP_003233894.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31502; -.
DR SMR; O31502; -.
DR IntAct; O31502; 2.
DR STRING; 224308.BSU06720; -.
DR SwissLipids; SLP:000001808; -.
DR PaxDb; O31502; -.
DR PRIDE; O31502; -.
DR EnsemblBacteria; CAB12492; CAB12492; BSU_06720.
DR GeneID; 936061; -.
DR KEGG; bsu:BSU06720; -.
DR PATRIC; fig|224308.179.peg.730; -.
DR eggNOG; COG1597; Bacteria.
DR InParanoid; O31502; -.
DR OMA; GFDSRVN; -.
DR PhylomeDB; O31502; -.
DR BioCyc; BSUB:BSU06720-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:CACAO.
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 1: Evidence at protein level;
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..303
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000386482"
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 9..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 66..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 93
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 303 AA; 33337 MW; 533F3658A41A5998 CRC64;
MKRARIIYNP TSGREIFKKH LAQVLQKFEQ AGYETSTHAT TCAGDATHAA KEAALREFDL
IIAAGGDGTI NEVVNGLAPL DNRPTLGVIP VGTTNDFARA LGIPREDILK AADTVINGVA
RPIDIGQVNG QYFINIAGGG RLTELTYDVP SKLKTMLGQL AYYLKGMEML PSLRPTEVEI
EYDGKLFQGE IMLFLVTLTN SVGGFEKLAP DSSLNDGMFD LMILKKANLA EFIRVATMAL
RGEHINDQHI IYTKANRVKV NVSEKMQLNL DGEYGGMLPG EFVNLYRHIH VVMPKEKAEQ
LDD
