ID   KDGL_SINSX              Reviewed;         137 AA.
AC   P29945;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1917841; DOI=10.1128/jb.173.19.6066-6073.1991;
RA   Cameron B., Blanche F., Rouyez M.-C., Bisch D., Famechon A., Couder M.,
RA   Cauchois L., Thibaut D., Debussche L., Crouzet J.;
RT   "Genetic analysis, nucleotide sequence, and products of two Pseudomonas
RT   denitrificans cob genes encoding nicotinate-nucleotide:
RT   dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5'-
RT   phosphate) synthase.";
RL   J. Bacteriol. 173:6066-6073(1991).
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   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M62868; AAA25789.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29945; -.
DR   SMR; P29945; -.
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   CHAIN           1..137
FT                   /note="Diacylglycerol kinase"
FT                   /id="PRO_0000195266"
FT   TRANSMEM        49..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABN1"
FT   BINDING         42
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABN1"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABN1"
SQ   SEQUENCE   137 AA;  14802 MW;  796675BA2D2C773F CRC64;
     MDAKNTTHRI GQTGPVEKQT GIRHLFAAAS YSLGGAKRLI GEAAFRHELI AFAAAMIAFI
     IVGATFFQYV AMAILFLLMM AFEAINTAIE EIVDRVSPEI SEMGKNAKDL GSFACLCLIV
     ANGVYAAYVV IFDGFMN