KDGL_SHIFL
ID KDGL_SHIFL Reviewed; 122 AA.
AC P0ABN4; P00556;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=SF4163, S3568;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45585.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18614.1; -; Genomic_DNA.
DR RefSeq; NP_709878.1; NC_004337.2.
DR RefSeq; WP_000002907.1; NZ_WPGW01000150.1.
DR AlphaFoldDB; P0ABN4; -.
DR BMRB; P0ABN4; -.
DR SMR; P0ABN4; -.
DR STRING; 198214.SF4163; -.
DR EnsemblBacteria; AAN45585; AAN45585; SF4163.
DR EnsemblBacteria; AAP18614; AAP18614; S3568.
DR GeneID; 1023428; -.
DR GeneID; 66672043; -.
DR KEGG; sfl:SF4163; -.
DR KEGG; sfx:S3568; -.
DR PATRIC; fig|198214.7.peg.4911; -.
DR HOGENOM; CLU_112343_3_1_6; -.
DR OMA; ITNEWHE; -.
DR OrthoDB; 2028997at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..122
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000195268"
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
