UniProt functional annotation for P0ABN1



	UniProt functional annotation for P0ABN1

UniProt code: P0ABN1.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2- diacylglycerol (DAG) to phosphatidic acid (PubMed:218816, PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:2828054, PubMed:9305868). Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis (PubMed:217867, PubMed:6305970). In vitro, phosphorylates various substrates, including sn-1,2- dioleoylglycerol, sn-1,2-dioctanoylglycerol, sn-1,2- dipalmitoylglycerol, sn-1,2-dipalmitate and ceramide (PubMed:218816, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). Catalyzes direct phosphoryl transfer from Mg-ATP to diacylglycerol and does not form an enzyme-phosphate intermediate (PubMed:9305868). {ECO:0000269|PubMed:217867, ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764, ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:6305970, ECO:0000269|PubMed:9305868}.

Catalytic activity: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3- phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868};

Catalytic activity: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z- octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3009449}; Note=Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser extents. {ECO:0000269|PubMed:3009449};

Activity regulation: Requires a lipid activator for activity. Activation is observed with cardiolipin and a large number of phospholipids, sulfolipids, neutral lipids, fatty acids, alkylglycosides or detergents (PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). A lipid cofactor-induced conformational change may occur as part of the activation process (PubMed:3021764). Requires a second divalent cation in addition to Mg(2+)-ATP (PubMed:3009449). Inhibited by the tetraphosphate-linked ATP-DAG bisubstrate analog (PubMed:9305868). {ECO:0000269|PubMed:2828054, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:3009449, ECO:0000269|PubMed:3021764, ECO:0000269|PubMed:6277376, ECO:0000269|PubMed:6303781, ECO:0000269|PubMed:9305868}.

Biophysicochemical properties: Kinetic parameters: KM=62 uM for sn-1,2-dipalmitate {ECO:0000269|PubMed:218816}; KM=230 uM for ceramide {ECO:0000269|PubMed:218816}; KM=1400 uM for ATP {ECO:0000269|PubMed:218816}; KM=300 uM for ATP {ECO:0000269|PubMed:3009449}; KM=120 uM for ATP {ECO:0000269|PubMed:10220339}; Vmax=10.4 umol/min/mg enzyme {ECO:0000269|PubMed:3009449}; Vmax=48 umol/min/mg enzyme with DAG as substrate {ECO:0000269|PubMed:10220339}; pH dependence: Optimum pH is 6.3-8.3. {ECO:0000269|PubMed:218816}; Temperature dependence: Apoprotein in organic solution has an unusual stability towards heating to 100 degrees Celsius. {ECO:0000269|PubMed:2828054};

Subunit: Homotrimer. {ECO:0000269|PubMed:19556511, ECO:0000269|PubMed:23676677, ECO:0000269|PubMed:25012698, ECO:0000269|PubMed:26673816, ECO:0000269|PubMed:9168044}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:217867, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:8071224}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:8071224}.

Induction: Expression is activated by the two-component system BasRS. Repressed by sigma-E factor. {ECO:0000269|PubMed:21463370}.

Domain: Contains three transmembrane helices and a N-terminal amphiphilic helix located on the cytoplasmic surface (PubMed:23676677, PubMed:26673816). Residues from different subunits participate in forming the active site (PubMed:10220339, PubMed:23676677). Contains three catalytic and substrate-binding sites centred about the membrane/cytosol interface (PubMed:26673816). The gamma-phosphate of the ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane (PubMed:26673816). {ECO:0000269|PubMed:10220339, ECO:0000269|PubMed:23676677, ECO:0000269|PubMed:26673816}.

Domain: The presence of Trp residues has a clear effect on thermal stability. Of the mutants containing a single Trp residue, only that containing Trp-113 was found to give active protein. {ECO:0000269|PubMed:12974643}.

Disruption phenotype: Mutant lacking this gene accumulates substantial amounts of diglyceride in the cytoplasmic membrane (PubMed:206553, PubMed:217867). Mutant also accumulates monoglyceride and triglyceride. Monoglyceride accumulates predominantly in the outer membrane, while triglyceride builds up together with diglyceride in the cytoplasmic membrane (PubMed:6305970). {ECO:0000269|PubMed:206553, ECO:0000269|PubMed:217867, ECO:0000269|PubMed:6305970}.

Miscellaneous: This small kinase has long served as a model for investigating membrane protein enzymology, folding, assembly and stability. {ECO:0000305}.

Similarity: Belongs to the bacterial diacylglycerol kinase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Catalyzes the ATP-dependent phosphorylation of sn-l,2- diacylglycerol (DAG) to phosphatidic acid (PubMed:218816, PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:2828054, PubMed:9305868). Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis (PubMed:217867, PubMed:6305970). In vitro, phosphorylates various substrates, including sn-1,2- dioleoylglycerol, sn-1,2-dioctanoylglycerol, sn-1,2- dipalmitoylglycerol, sn-1,2-dipalmitate and ceramide (PubMed:218816, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). Catalyzes direct phosphoryl transfer from Mg-ATP to diacylglycerol and does not form an enzyme-phosphate intermediate (PubMed:9305868). {ECO:0000269\|PubMed:217867, ECO:0000269\|PubMed:218816, ECO:0000269\|PubMed:2828054, ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:3009449, ECO:0000269\|PubMed:3021764, ECO:0000269\|PubMed:6277376, ECO:0000269\|PubMed:6303781, ECO:0000269\|PubMed:6305970, ECO:0000269\|PubMed:9305868}.


Catalytic activity:		Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3- phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269\|PubMed:218816, ECO:0000269\|PubMed:2828054, ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:6277376, ECO:0000269\|PubMed:6303781, ECO:0000269\|PubMed:9305868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000269\|PubMed:218816, ECO:0000269\|PubMed:2828054, ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:6277376, ECO:0000269\|PubMed:6303781, ECO:0000269\|PubMed:9305868};
Catalytic activity:		Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z- octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:3009449, ECO:0000269\|PubMed:3021764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:3009449, ECO:0000269\|PubMed:3021764};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:3009449}; Note=Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser extents. {ECO:0000269\|PubMed:3009449};
Activity regulation:		Requires a lipid activator for activity. Activation is observed with cardiolipin and a large number of phospholipids, sulfolipids, neutral lipids, fatty acids, alkylglycosides or detergents (PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). A lipid cofactor-induced conformational change may occur as part of the activation process (PubMed:3021764). Requires a second divalent cation in addition to Mg(2+)-ATP (PubMed:3009449). Inhibited by the tetraphosphate-linked ATP-DAG bisubstrate analog (PubMed:9305868). {ECO:0000269\|PubMed:2828054, ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:3009449, ECO:0000269\|PubMed:3021764, ECO:0000269\|PubMed:6277376, ECO:0000269\|PubMed:6303781, ECO:0000269\|PubMed:9305868}.
Biophysicochemical properties:		Kinetic parameters: KM=62 uM for sn-1,2-dipalmitate {ECO:0000269\|PubMed:218816}; KM=230 uM for ceramide {ECO:0000269\|PubMed:218816}; KM=1400 uM for ATP {ECO:0000269\|PubMed:218816}; KM=300 uM for ATP {ECO:0000269\|PubMed:3009449}; KM=120 uM for ATP {ECO:0000269\|PubMed:10220339}; Vmax=10.4 umol/min/mg enzyme {ECO:0000269\|PubMed:3009449}; Vmax=48 umol/min/mg enzyme with DAG as substrate {ECO:0000269\|PubMed:10220339}; pH dependence: Optimum pH is 6.3-8.3. {ECO:0000269\|PubMed:218816}; Temperature dependence: Apoprotein in organic solution has an unusual stability towards heating to 100 degrees Celsius. {ECO:0000269\|PubMed:2828054};
Subunit:		Homotrimer. {ECO:0000269\|PubMed:19556511, ECO:0000269\|PubMed:23676677, ECO:0000269\|PubMed:25012698, ECO:0000269\|PubMed:26673816, ECO:0000269\|PubMed:9168044}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:15919996, ECO:0000269\|PubMed:217867, ECO:0000269\|PubMed:2984194, ECO:0000269\|PubMed:8071224}; Multi-pass membrane protein {ECO:0000255, ECO:0000269\|PubMed:8071224}.
Induction:		Expression is activated by the two-component system BasRS. Repressed by sigma-E factor. {ECO:0000269\|PubMed:21463370}.
Domain:		Contains three transmembrane helices and a N-terminal amphiphilic helix located on the cytoplasmic surface (PubMed:23676677, PubMed:26673816). Residues from different subunits participate in forming the active site (PubMed:10220339, PubMed:23676677). Contains three catalytic and substrate-binding sites centred about the membrane/cytosol interface (PubMed:26673816). The gamma-phosphate of the ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane (PubMed:26673816). {ECO:0000269\|PubMed:10220339, ECO:0000269\|PubMed:23676677, ECO:0000269\|PubMed:26673816}.
Domain:		The presence of Trp residues has a clear effect on thermal stability. Of the mutants containing a single Trp residue, only that containing Trp-113 was found to give active protein. {ECO:0000269\|PubMed:12974643}.
Disruption phenotype:		Mutant lacking this gene accumulates substantial amounts of diglyceride in the cytoplasmic membrane (PubMed:206553, PubMed:217867). Mutant also accumulates monoglyceride and triglyceride. Monoglyceride accumulates predominantly in the outer membrane, while triglyceride builds up together with diglyceride in the cytoplasmic membrane (PubMed:6305970). {ECO:0000269\|PubMed:206553, ECO:0000269\|PubMed:217867, ECO:0000269\|PubMed:6305970}.
Miscellaneous:		This small kinase has long served as a model for investigating membrane protein enzymology, folding, assembly and stability. {ECO:0000305}.
Similarity:		Belongs to the bacterial diacylglycerol kinase family. {ECO:0000305}.