KDGL_ECOLI
ID KDGL_ECOLI Reviewed; 122 AA.
AC P0ABN1; P00556; Q2M6R2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Diacylglycerol kinase {ECO:0000303|PubMed:6303781};
DE Short=DAGK {ECO:0000303|PubMed:8071224};
DE EC=2.7.1.107 {ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868};
DE AltName: Full=Diglyceride kinase {ECO:0000303|PubMed:206553};
DE Short=DGK {ECO:0000305};
GN Name=dgkA {ECO:0000303|PubMed:2984194};
GN Synonyms=dgk {ECO:0000303|PubMed:206553}; OrderedLocusNames=b4042, JW4002;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6309817; DOI=10.1016/s0021-9258(17)44354-7;
RA Lightner V.A., Bell R.M., Modrich P.;
RT "The DNA sequences encoding plsB and dgk loci of Escherichia coli.";
RL J. Biol. Chem. 258:10856-10861(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=2984194; DOI=10.1016/s0021-9258(18)89235-3;
RA Loomis C.R., Walsh J.P., Bell R.M.;
RT "sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification,
RT reconstitution, and partial amino- and carboxyl-terminal analysis.";
RL J. Biol. Chem. 260:4091-4097(1985).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=206553; DOI=10.1016/s0021-9258(17)34773-7;
RA Raetz C.R., Newman K.F.;
RT "Neutral lipid accumulation in the membranes of Escherichia coli mutants
RT lacking diglyceride kinase.";
RL J. Biol. Chem. 253:3882-3887(1978).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=217867; DOI=10.1128/jb.137.2.860-868.1979;
RA Raetz C.R., Newman K.F.;
RT "Diglyceride kinase mutants of Escherichia coli: inner membrane association
RT of 1,2-diglyceride and its relation to synthesis of membrane-derived
RT oligosaccharides.";
RL J. Bacteriol. 137:860-868(1979).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=218816; DOI=10.1111/j.1432-1033.1979.tb12907.x;
RA Bohnenberger E., Sandermann H. Jr.;
RT "Diglyceride kinase from Escherichia coli. Purification in organic solvent
RT and some properties of the enzyme.";
RL Eur. J. Biochem. 94:401-407(1979).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=6277376; DOI=10.1016/0005-2736(82)90033-5;
RA Bohnenberger E., Sandermann H. Jr.;
RT "Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by
RT glycosphingolipids.";
RL Biochim. Biophys. Acta 685:44-50(1982).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=6303781; DOI=10.1111/j.1432-1033.1983.tb07412.x;
RA Bohnenberger E., Sandermann H. Jr.;
RT "Lipid dependence of diacylglycerol kinase from Escherichia coli.";
RL Eur. J. Biochem. 132:645-650(1983).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6305970; DOI=10.1016/s0021-9258(20)82028-6;
RA Rotering H., Raetz C.R.;
RT "Appearance of monoglyceride and triglyceride in the cell envelope of
RT Escherichia coli mutants defective in diglyceride kinase.";
RL J. Biol. Chem. 258:8068-8073(1983).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3009449; DOI=10.1016/s0021-9258(19)84554-4;
RA Walsh J.P., Bell R.M.;
RT "sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis
RT of the phospholipid cofactor requirement and divalent cation dependence.";
RL J. Biol. Chem. 261:6239-6247(1986).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=3021764; DOI=10.1016/s0021-9258(18)66830-9;
RA Walsh J.P., Bell R.M.;
RT "sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic
RT analysis of the lipid cofactor dependence.";
RL J. Biol. Chem. 261:15062-15069(1986).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=2828054; DOI=10.1111/j.1432-1033.1988.tb13795.x;
RA Russ E., Kaiser U., Sandermann H. Jr.;
RT "Lipid-dependent membrane enzymes. Purification to homogeneity and further
RT characterization of diacylglycerol kinase from Escherichia coli.";
RL Eur. J. Biochem. 171:335-342(1988).
RN [15]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=8071224; DOI=10.1128/jb.176.17.5459-5465.1994;
RA Smith R.L., O'Toole J.F., Maguire M.E., Sanders C.R. II;
RT "Membrane topology of Escherichia coli diacylglycerol kinase.";
RL J. Bacteriol. 176:5459-5465(1994).
RN [16]
RP SUBUNIT.
RX PubMed=9168044; DOI=10.1016/s0006-3495(97)78912-4;
RA Vinogradova O., Badola P., Czerski L., Soennichsen F.D., Sanders C.R. II;
RT "Escherichia coli diacylglycerol kinase: a case study in the application of
RT solution NMR methods to an integral membrane protein.";
RL Biophys. J. 72:2688-2701(1997).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND ACTIVITY REGULATION.
RX PubMed=9305868; DOI=10.1074/jbc.272.39.24176;
RA Badola P., Sanders C.R. II;
RT "Escherichia coli diacylglycerol kinase is an evolutionarily optimized
RT membrane enzyme and catalyzes direct phosphoryl transfer.";
RL J. Biol. Chem. 272:24176-24182(1997).
RN [18]
RP DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ALA-15; GLU-70;
RP ASN-73; GLU-77; LYS-95 AND ASP-96.
RX PubMed=10220339; DOI=10.1021/bi982763t;
RA Lau F.W., Chen X., Bowie J.U.;
RT "Active sites of diacylglycerol kinase from Escherichia coli are shared
RT between subunits.";
RL Biochemistry 38:5521-5527(1999).
RN [19]
RP TOPOLOGY OF THE N-TERMINAL REGION.
RX PubMed=12379131; DOI=10.1021/bi020335o;
RA Oxenoid K., Soennichsen F.D., Sanders C.R.;
RT "Topology and secondary structure of the N-terminal domain of
RT diacylglycerol kinase.";
RL Biochemistry 41:12876-12882(2002).
RN [20]
RP DOMAIN, AND MUTAGENESIS OF TRP-19 AND TRP-26.
RX PubMed=12974643; DOI=10.1021/bi034607e;
RA Clark E.H., East J.M., Lee A.G.;
RT "The role of tryptophan residues in an integral membrane protein:
RT diacylglycerol kinase.";
RL Biochemistry 42:11065-11073(2003).
RN [21]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [22]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=21463370; DOI=10.1111/j.1365-2958.2011.07641.x;
RA Wahl A., My L., Dumoulin R., Sturgis J.N., Bouveret E.;
RT "Antagonistic regulation of dgkA and plsB genes of phospholipid synthesis
RT by multiple stress responses in Escherichia coli.";
RL Mol. Microbiol. 80:1260-1275(2011).
RN [23] {ECO:0007744|PDB:2KDC}
RP STRUCTURE BY NMR OF 2-122, AND SUBUNIT.
RX PubMed=19556511; DOI=10.1126/science.1171716;
RA Van Horn W.D., Kim H.J., Ellis C.D., Hadziselimovic A., Sulistijo E.S.,
RA Karra M.D., Tian C., Sonnichsen F.D., Sanders C.R.;
RT "Solution nuclear magnetic resonance structure of membrane-integral
RT diacylglycerol kinase.";
RL Science 324:1726-1729(2009).
RN [24] {ECO:0007744|PDB:3ZE3, ECO:0007744|PDB:3ZE4, ECO:0007744|PDB:3ZE5}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-122 OF APOENZYME AND IN COMPLEX
RP WITH ZINC AND 7.8 MONOACYLGLYCEROL, SUBUNIT, AND DOMAIN.
RX PubMed=23676677; DOI=10.1038/nature12179;
RA Li D., Lyons J.A., Pye V.E., Vogeley L., Aragao D., Kenyon C.P., Shah S.T.,
RA Doherty C., Aherne M., Caffrey M.;
RT "Crystal structure of the integral membrane diacylglycerol kinase.";
RL Nature 497:521-524(2013).
RN [25] {ECO:0007744|PDB:4BRR}
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 2-122 IN COMPLEX WITH ZINC AND
RP SUBSTRATE ANALOG.
RA Li D., Howe N., Caffrey M.;
RT "Crystal structure of an integral membrane enzyme determined by X-ray free
RT electron laser femtocrystallography.";
RL Submitted (JUN-2013) to the PDB data bank.
RN [26] {ECO:0007744|PDB:4CJZ, ECO:0007744|PDB:4CK0}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC;
RP OLEOYL-R-GLYCEROL AND ATP ANALOG.
RA Li D., Caffrey M.;
RT "Crystal structure of the integral membrane diacylglycerol kinase with Zn-
RT Amppcp bound and its catalytic mechanism.";
RL Submitted (DEC-2013) to the PDB data bank.
RN [27] {ECO:0007744|PDB:4BPD, ECO:0007744|PDB:4D2E}
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC AND
RP 7.8 MONOACYLGLYCEROL, AND SUBUNIT.
RX PubMed=25012698; DOI=10.1007/s00018-014-1655-7;
RA Boland C., Li D., Shah S.T.A., Haberstock S., Dotsch V., Bernhard F.,
RA Caffrey M.;
RT "Cell-free expression and in meso crystallisation of an integral membrane
RT kinase for structure determination.";
RL Cell. Mol. Life Sci. 71:4895-4910(2014).
RN [28] {ECO:0007744|PDB:4BRB, ECO:0007744|PDB:4UP6}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-122 OF APOENZYME AND IN COMPLEX
RP WITH ZINC AND 7.8 MONOACYLGLYCEROL.
RX PubMed=25055873; DOI=10.1038/srep05806;
RA Li D., Caffrey M.;
RT "Renaturing membrane proteins in the lipid cubic phase, a nanoporous
RT membrane mimetic.";
RL Sci. Rep. 4:5806-5806(2014).
RN [29] {ECO:0007744|PDB:4UXW, ECO:0007744|PDB:4UXX, ECO:0007744|PDB:4UXZ, ECO:0007744|PDB:4UYO}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC;
RP MONOACYLGLYCEROLS AND ATP ANALOG, REACTION MECHANISM, SUBUNIT, DOMAIN,
RP ACTIVE SITE, AND MUTAGENESIS OF ALA-31; GLU-70; ASN-73; GLY-84 AND ASP-96.
RX PubMed=26673816; DOI=10.1038/ncomms10140;
RA Li D., Stansfeld P.J., Sansom M.S.P., Keogh A., Vogeley L., Howe N.,
RA Lyons J.A., Aragao D., Fromme P., Fromme R., Basu S., Grotjohann I.,
RA Kupitz C., Rendek K., Weierstall U., Zatsepin N.A., Cherezov V., Liu W.,
RA Bandaru S., English N.J., Gati C., Barty A., Yefanov O., Chapman H.N.,
RA Diederichs K., Messerschmidt M., Boutet S., Williams G.J.,
RA Marvin Seibert M., Caffrey M.;
RT "Ternary structure reveals mechanism of a membrane diacylglycerol kinase.";
RL Nat. Commun. 6:10140-10140(2015).
RN [30] {ECO:0007744|PDB:5DWK}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-122 IN COMPLEX WITH ZINC AND
RP 7.8 MONOACYLGLYCEROL.
RX PubMed=26960129; DOI=10.1107/s2059798315024110;
RA Olieric V., Weinert T., Finke A.D., Anders C., Li D., Olieric N.,
RA Borca C.N., Steinmetz M.O., Caffrey M., Jinek M., Wang M.;
RT "Data-collection strategy for challenging native SAD phasing.";
RL Acta Crystallogr. D 72:421-429(2016).
RN [31] {ECO:0007744|PDB:5D56, ECO:0007744|PDB:5D57}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-122 IN COMPLEX WITH ZINC AND
RP 7.8 MONOACYLGLYCEROL.
RX PubMed=26894538; DOI=10.1107/s2059798315021683;
RA Huang C.Y., Olieric V., Ma P., Howe N., Vogeley L., Liu X.,
RA Warshamanage R., Weinert T., Panepucci E., Kobilka B., Diederichs K.,
RA Wang M., Caffrey M.;
RT "In meso in situ serial X-ray crystallography of soluble and membrane
RT proteins at cryogenic temperatures.";
RL Acta Crystallogr. D 72:93-112(2016).
RN [32] {ECO:0007744|PDB:5D6I}
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS).
RX PubMed=28771236; DOI=10.1038/nprot.2017.057;
RA Ma P., Weichert D., Aleksandrov L.A., Jensen T.J., Riordan J.R., Liu X.,
RA Kobilka B.K., Caffrey M.;
RT "The cubicon method for concentrating membrane proteins in the cubic
RT mesophase.";
RL Nat. Protoc. 12:1745-1762(2017).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of sn-l,2-
CC diacylglycerol (DAG) to phosphatidic acid (PubMed:218816,
CC PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449,
CC PubMed:2828054, PubMed:9305868). Involved in the recycling of
CC diacylglycerol produced as a by-product during membrane-derived
CC oligosaccharide (MDO) biosynthesis (PubMed:217867, PubMed:6305970). In
CC vitro, phosphorylates various substrates, including sn-1,2-
CC dioleoylglycerol, sn-1,2-dioctanoylglycerol, sn-1,2-
CC dipalmitoylglycerol, sn-1,2-dipalmitate and ceramide (PubMed:218816,
CC PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054).
CC Catalyzes direct phosphoryl transfer from Mg-ATP to diacylglycerol and
CC does not form an enzyme-phosphate intermediate (PubMed:9305868).
CC {ECO:0000269|PubMed:217867, ECO:0000269|PubMed:218816,
CC ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194,
CC ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764,
CC ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781,
CC ECO:0000269|PubMed:6305970, ECO:0000269|PubMed:9305868}.
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:218816, ECO:0000269|PubMed:2828054,
CC ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:6277376,
CC ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054,
CC ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:6277376,
CC ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868};
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:2984194, ECO:0000269|PubMed:3009449,
CC ECO:0000269|PubMed:3021764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:3009449,
CC ECO:0000269|PubMed:3021764};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3009449};
CC Note=Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser
CC extents. {ECO:0000269|PubMed:3009449};
CC -!- ACTIVITY REGULATION: Requires a lipid activator for activity.
CC Activation is observed with cardiolipin and a large number of
CC phospholipids, sulfolipids, neutral lipids, fatty acids,
CC alkylglycosides or detergents (PubMed:6277376, PubMed:6303781,
CC PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). A
CC lipid cofactor-induced conformational change may occur as part of the
CC activation process (PubMed:3021764). Requires a second divalent cation
CC in addition to Mg(2+)-ATP (PubMed:3009449). Inhibited by the
CC tetraphosphate-linked ATP-DAG bisubstrate analog (PubMed:9305868).
CC {ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194,
CC ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764,
CC ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781,
CC ECO:0000269|PubMed:9305868}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 uM for sn-1,2-dipalmitate {ECO:0000269|PubMed:218816};
CC KM=230 uM for ceramide {ECO:0000269|PubMed:218816};
CC KM=1400 uM for ATP {ECO:0000269|PubMed:218816};
CC KM=300 uM for ATP {ECO:0000269|PubMed:3009449};
CC KM=120 uM for ATP {ECO:0000269|PubMed:10220339};
CC Vmax=10.4 umol/min/mg enzyme {ECO:0000269|PubMed:3009449};
CC Vmax=48 umol/min/mg enzyme with DAG as substrate
CC {ECO:0000269|PubMed:10220339};
CC pH dependence:
CC Optimum pH is 6.3-8.3. {ECO:0000269|PubMed:218816};
CC Temperature dependence:
CC Apoprotein in organic solution has an unusual stability towards
CC heating to 100 degrees Celsius. {ECO:0000269|PubMed:2828054};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19556511,
CC ECO:0000269|PubMed:23676677, ECO:0000269|PubMed:25012698,
CC ECO:0000269|PubMed:26673816, ECO:0000269|PubMed:9168044}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:217867, ECO:0000269|PubMed:2984194,
CC ECO:0000269|PubMed:8071224}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:8071224}.
CC -!- INDUCTION: Expression is activated by the two-component system BasRS.
CC Repressed by sigma-E factor. {ECO:0000269|PubMed:21463370}.
CC -!- DOMAIN: Contains three transmembrane helices and a N-terminal
CC amphiphilic helix located on the cytoplasmic surface (PubMed:23676677,
CC PubMed:26673816). Residues from different subunits participate in
CC forming the active site (PubMed:10220339, PubMed:23676677). Contains
CC three catalytic and substrate-binding sites centred about the
CC membrane/cytosol interface (PubMed:26673816). The gamma-phosphate of
CC the ATP is positioned for direct transfer to the primary hydroxyl of
CC the lipid whose acyl chain is in the membrane (PubMed:26673816).
CC {ECO:0000269|PubMed:10220339, ECO:0000269|PubMed:23676677,
CC ECO:0000269|PubMed:26673816}.
CC -!- DOMAIN: The presence of Trp residues has a clear effect on thermal
CC stability. Of the mutants containing a single Trp residue, only that
CC containing Trp-113 was found to give active protein.
CC {ECO:0000269|PubMed:12974643}.
CC -!- DISRUPTION PHENOTYPE: Mutant lacking this gene accumulates substantial
CC amounts of diglyceride in the cytoplasmic membrane (PubMed:206553,
CC PubMed:217867). Mutant also accumulates monoglyceride and triglyceride.
CC Monoglyceride accumulates predominantly in the outer membrane, while
CC triglyceride builds up together with diglyceride in the cytoplasmic
CC membrane (PubMed:6305970). {ECO:0000269|PubMed:206553,
CC ECO:0000269|PubMed:217867, ECO:0000269|PubMed:6305970}.
CC -!- MISCELLANEOUS: This small kinase has long served as a model for
CC investigating membrane protein enzymology, folding, assembly and
CC stability. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; K00127; AAA24394.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43136.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77012.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78044.1; -; Genomic_DNA.
DR PIR; A00667; KIECDG.
DR RefSeq; NP_418466.1; NC_000913.3.
DR RefSeq; WP_000002907.1; NZ_STEB01000022.1.
DR PDB; 2KDC; NMR; -; A/B/C=2-122.
DR PDB; 3ZE3; X-ray; 2.05 A; A/B/C/D/E/F=2-122.
DR PDB; 3ZE4; X-ray; 3.70 A; A/B/C=2-122.
DR PDB; 3ZE5; X-ray; 3.10 A; A/B/C=2-122.
DR PDB; 4BPD; X-ray; 3.30 A; A/B/C/D/E/F=2-122.
DR PDB; 4BRB; X-ray; 2.55 A; A/B/C/D/E/F=2-122.
DR PDB; 4BRR; X-ray; 2.44 A; A/B/C/D/E/F=2-122.
DR PDB; 4CJZ; X-ray; 3.25 A; A/B/C=2-122.
DR PDB; 4CK0; X-ray; 2.92 A; A/B/C=2-122.
DR PDB; 4D2E; X-ray; 2.28 A; A/B/C/D/E/F=2-122.
DR PDB; 4UP6; X-ray; 3.80 A; A/B/C=2-122.
DR PDB; 4UXW; X-ray; 3.15 A; A/B/C=2-122.
DR PDB; 4UXX; X-ray; 2.70 A; A/B/C=2-122.
DR PDB; 4UXZ; X-ray; 2.18 A; A/B/C/D/E/F=2-122.
DR PDB; 4UYO; X-ray; 2.18 A; A/B/C/D/E/F=2-122.
DR PDB; 5D56; X-ray; 2.80 A; A/B/C/D/E/F=2-122.
DR PDB; 5D57; X-ray; 2.80 A; A/B/C/D/E/F=2-122.
DR PDB; 5D6I; X-ray; 3.09 A; A/B/C=2-122.
DR PDB; 5DWK; X-ray; 2.60 A; A/B/C/D/E/F=2-122.
DR PDBsum; 2KDC; -.
DR PDBsum; 3ZE3; -.
DR PDBsum; 3ZE4; -.
DR PDBsum; 3ZE5; -.
DR PDBsum; 4BPD; -.
DR PDBsum; 4BRB; -.
DR PDBsum; 4BRR; -.
DR PDBsum; 4CJZ; -.
DR PDBsum; 4CK0; -.
DR PDBsum; 4D2E; -.
DR PDBsum; 4UP6; -.
DR PDBsum; 4UXW; -.
DR PDBsum; 4UXX; -.
DR PDBsum; 4UXZ; -.
DR PDBsum; 4UYO; -.
DR PDBsum; 5D56; -.
DR PDBsum; 5D57; -.
DR PDBsum; 5D6I; -.
DR PDBsum; 5DWK; -.
DR AlphaFoldDB; P0ABN1; -.
DR BMRB; P0ABN1; -.
DR SMR; P0ABN1; -.
DR BioGRID; 4261719; 281.
DR BioGRID; 852837; 2.
DR DIP; DIP-60228N; -.
DR STRING; 511145.b4042; -.
DR SwissLipids; SLP:000001806; -.
DR jPOST; P0ABN1; -.
DR PaxDb; P0ABN1; -.
DR PRIDE; P0ABN1; -.
DR EnsemblBacteria; AAC77012; AAC77012; b4042.
DR EnsemblBacteria; BAE78044; BAE78044; BAE78044.
DR GeneID; 66672043; -.
DR GeneID; 948543; -.
DR KEGG; ecj:JW4002; -.
DR KEGG; eco:b4042; -.
DR PATRIC; fig|1411691.4.peg.2666; -.
DR EchoBASE; EB0220; -.
DR eggNOG; COG0818; Bacteria.
DR HOGENOM; CLU_112343_3_1_6; -.
DR InParanoid; P0ABN1; -.
DR OMA; ITNEWHE; -.
DR PhylomeDB; P0ABN1; -.
DR BioCyc; EcoCyc:DIACYLGLYKIN-MON; -.
DR BioCyc; MetaCyc:DIACYLGLYKIN-MON; -.
DR BRENDA; 2.7.1.107; 2026.
DR SABIO-RK; P0ABN1; -.
DR EvolutionaryTrace; P0ABN1; -.
DR PRO; PR:P0ABN1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR CDD; cd14264; DAGK_IM; 1.
DR Gene3D; 1.10.287.3610; -; 1.
DR InterPro; IPR000829; DAGK.
DR InterPro; IPR033718; DAGK_prok.
DR InterPro; IPR036945; DAGK_sf.
DR PANTHER; PTHR34299; PTHR34299; 1.
DR Pfam; PF01219; DAGK_prokar; 1.
DR PROSITE; PS01069; DAGK_PROKAR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2984194"
FT CHAIN 2..122
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000195260"
FT TOPO_DOM 2..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8071224"
FT TRANSMEM 32..48
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12379131,
FT ECO:0000305|PubMed:8071224"
FT TOPO_DOM 49..51
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:12379131,
FT ECO:0000305|PubMed:8071224"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12379131,
FT ECO:0000305|PubMed:8071224"
FT TOPO_DOM 70..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8071224"
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8071224"
FT TOPO_DOM 120..122
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:8071224"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:26673816"
FT BINDING 10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25012698,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538"
FT BINDING 14..19
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538,
FT ECO:0000305|PubMed:26960129"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 23..26
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:23676677,
FT ECO:0000269|PubMed:25012698, ECO:0000269|PubMed:26673816,
FT ECO:0000269|PubMed:26894538, ECO:0000269|PubMed:26960129,
FT ECO:0000269|Ref.25"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 31..35
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538,
FT ECO:0000305|PubMed:26960129"
FT BINDING 48..51
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816,
FT ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129,
FT ECO:0000305|Ref.25"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538,
FT ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25012698,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538,
FT ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26"
FT BINDING 77
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:23676677,
FT ECO:0000269|PubMed:25012698, ECO:0000269|PubMed:26673816,
FT ECO:0000269|PubMed:26894538, ECO:0000269|PubMed:26960129,
FT ECO:0000269|Ref.25"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 86..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 95..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816,
FT ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129"
FT BINDING 113..118
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:23676677,
FT ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873,
FT ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538,
FT ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26"
FT MUTAGEN 15
FT /note="A->Q: 49% of wild-type specific activity.
FT Inactivates wild-type subunits; when associated with S-73."
FT /evidence="ECO:0000269|PubMed:10220339"
FT MUTAGEN 19
FT /note="W->L: 60% of wild-type activity. 41% of wild-type
FT activity; when associated with L-26."
FT /evidence="ECO:0000269|PubMed:12974643"
FT MUTAGEN 26
FT /note="W->L: 23% of wild-type activity. 41% of wild-type
FT activity; when associated with L-19."
FT /evidence="ECO:0000269|PubMed:12974643"
FT MUTAGEN 31
FT /note="A->L: 93% decrease in activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 70
FT /note="E->A,D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 70
FT /note="E->C: 50% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:10220339"
FT MUTAGEN 73
FT /note="N->A,Q,D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 73
FT /note="N->S: 51% of wild-type specific activity.
FT Inactivates wild-type subunits; when associated with Q-15."
FT /evidence="ECO:0000269|PubMed:10220339"
FT MUTAGEN 77
FT /note="E->L: 51% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:10220339"
FT MUTAGEN 84
FT /note="G->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 95
FT /note="K->L: 54% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:10220339"
FT MUTAGEN 96
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 96
FT /note="D->E: 76% decrease in activity."
FT /evidence="ECO:0000269|PubMed:26673816"
FT MUTAGEN 96
FT /note="D->N: 27% of wild-type specific activity.
FT Inactivates wild-type subunits. Almost no change in
FT activity."
FT /evidence="ECO:0000269|PubMed:10220339,
FT ECO:0000269|PubMed:26673816"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:3ZE3"
FT HELIX 30..48
FT /evidence="ECO:0007829|PDB:3ZE3"
FT HELIX 53..83
FT /evidence="ECO:0007829|PDB:3ZE3"
FT HELIX 89..120
FT /evidence="ECO:0007829|PDB:3ZE3"
SQ SEQUENCE 122 AA; 13245 MW; D5B4F86925FA6A17 CRC64;
MANNTTGFTR IIKAAGYSWK GLRAAWINEA AFRQEGVAVL LAVVIACWLD VDAITRVLLI
SSVMLVMIVE ILNSAIEAVV DRIGSEYHEL SGRAKDMGSA AVLIAIIVAV ITWCILLWSH
FG
