ID KDGL_ECOL6 Reviewed; 122 AA. AC P0ABN2; P00556; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 98. DE RecName: Full=Diacylglycerol kinase {ECO:0000250|UniProtKB:P0ABN1}; DE Short=DAGK {ECO:0000250|UniProtKB:P0ABN1}; DE EC=2.7.1.107 {ECO:0000250|UniProtKB:P0ABN1}; DE AltName: Full=Diglyceride kinase {ECO:0000250|UniProtKB:P0ABN1}; DE Short=DGK {ECO:0000250|UniProtKB:P0ABN1}; GN Name=dgkA; OrderedLocusNames=c5013; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of sn-l,2- CC diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of CC diacylglycerol produced as a by-product during membrane-derived CC oligosaccharide (MDO) biosynthesis. {ECO:0000250|UniProtKB:P0ABN1}. 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:P0ABN1}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0ABN1}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0ABN1}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P0ABN1}. CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014075; AAN83439.1; -; Genomic_DNA. DR RefSeq; WP_000002907.1; NC_004431.1. DR AlphaFoldDB; P0ABN2; -. DR BMRB; P0ABN2; -. DR SMR; P0ABN2; -. DR STRING; 199310.c5013; -. DR GeneID; 93777789; -. DR KEGG; ecc:c5013; -. DR eggNOG; COG0818; Bacteria. DR HOGENOM; CLU_112343_3_1_6; -. DR BioCyc; ECOL199310:C5013-MONOMER; -. DR Proteomes; UP000001410; Chromosome. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; ISS:UniProtKB. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro. DR CDD; cd14264; DAGK_IM; 1. DR FunFam; 1.10.287.3610:FF:000001; Diacylglycerol kinase; 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; DIACYLGLYCEROL KINASE; 1. DR PANTHER; PTHR34299:SF1; DIACYLGLYCEROL KINASE; 1. DR Pfam; PF01219; DAGK_prokar; 1. DR PROSITE; PS01069; DAGK_PROKAR; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; KW Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..122 FT /note="Diacylglycerol kinase" FT /id="PRO_0000195262" FT TRANSMEM 35..55 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 10 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 14..19 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 23..26 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 29 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 31..35 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 48..51 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 77 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 86..88 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 95..96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" FT BINDING 113..118 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ABN1" SQ SEQUENCE 122 AA; 13245 MW; D5B4F86925FA6A17 CRC64; MANNTTGFTR IIKAAGYSWK GLRAAWINEA AFRQEGVAVL LAVVIACWLD VDAITRVLLI SSVMLVMIVE ILNSAIEAVV DRIGSEYHEL SGRAKDMGSA AVLIAIIVAV ITWCILLWSH FG //