KDGL_HELPJ
ID KDGL_HELPJ Reviewed; 128 AA.
AC Q9ZLE0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=jhp_0640;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06218.1; -; Genomic_DNA.
DR PIR; D71906; D71906.
DR RefSeq; WP_001279229.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZLE0; -.
DR SMR; Q9ZLE0; -.
DR STRING; 85963.jhp_0640; -.
DR EnsemblBacteria; AAD06218; AAD06218; jhp_0640.
DR KEGG; hpj:jhp_0640; -.
DR PATRIC; fig|85963.30.peg.344; -.
DR eggNOG; COG0818; Bacteria.
DR OMA; KCAWVEE; -.
DR Proteomes; UP000000804; 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 CHAIN 1..128
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000195265"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
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; 14598 MW; AC96B8630A8B1B7D CRC64;
MSDFKVPPKA KGFKRLFKAL FYSKDGLKCA WAEESAFRQI VILALFCIVL ASYLTKDFLE
WGLLILPCFL SVVIELINSS IEKAVDFTGT EFHPLAKKAK DMASSAQLIG LIFWAFIWGR
YLLTLYFN
