KDGL_HELPY
ID KDGL_HELPY Reviewed; 128 AA.
AC P56411;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=HP_0700;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07752.1; -; Genomic_DNA.
DR PIR; D64607; D64607.
DR RefSeq; NP_207494.1; NC_000915.1.
DR RefSeq; WP_001279026.1; NC_018939.1.
DR AlphaFoldDB; P56411; -.
DR SMR; P56411; -.
DR STRING; 85962.C694_03610; -.
DR PaxDb; P56411; -.
DR EnsemblBacteria; AAD07752; AAD07752; HP_0700.
DR KEGG; hpy:HP_0700; -.
DR PATRIC; fig|85962.47.peg.749; -.
DR eggNOG; COG0818; Bacteria.
DR OMA; KCAWVEE; -.
DR PhylomeDB; P56411; -.
DR Proteomes; UP000000429; 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 Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..128
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000195264"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0ABN1"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0ABN1"
FT BINDING 82
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0ABN1"
SQ SEQUENCE 128 AA; 14527 MW; F788FB3CFBDB59E8 CRC64;
MSDFEVPPKA KGFKRLFKAL FYSKDGLKCA WIEESAFRQI VILALFCIVL ASYLAKDFLE
WGLLILPCFL SVVVELINSS IEKAVDFTGT EFHPLAKKAK DMASAAQLIG LIFWTLIWGR
YLLALYLK
