KDGL_ECOL6
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 03-AUG-2022, entry version 84.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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 EnsemblBacteria; AAN83439; AAN83439; c5013.
DR GeneID; 66672043; -.
DR KEGG; ecc:c5013; -.
DR eggNOG; COG0818; Bacteria.
DR HOGENOM; CLU_112343_3_1_6; -.
DR OMA; ITNEWHE; -.
DR BioCyc; ECOL199310:C5013-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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 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
