ID   Q24SU5_DESHY            Unreviewed;       127 AA.
AC   Q24SU5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Diacylglycerol kinase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=DSY3108 {ECO:0000313|EMBL:BAE84897.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE84897.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE84897.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE84897.1,
RC   ECO:0000313|Proteomes:UP000001946};
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600829-4};
CC       Note=Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser
CC       extents. {ECO:0000256|PIRSR:PIRSR600829-4};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00005967}.
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DR   EMBL; AP008230; BAE84897.1; -; Genomic_DNA.
DR   RefSeq; WP_011460856.1; NC_007907.1.
DR   AlphaFoldDB; Q24SU5; -.
DR   STRING; 138119.DSY3108; -.
DR   KEGG; dsy:DSY3108; -.
DR   eggNOG; COG0818; Bacteria.
DR   HOGENOM; CLU_112343_2_2_9; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14265; UDPK_IM_like; 1.
DR   Gene3D; 1.10.287.3610; -; 1.
DR   InterPro; IPR000829; DAGK.
DR   InterPro; IPR036945; DAGK_sf.
DR   InterPro; IPR033717; UDPK.
DR   PANTHER; PTHR34299; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR34299:SF1; DIACYLGLYCEROL KINASE; 1.
DR   Pfam; PF01219; DAGK_prokar; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR600829-
KW   3}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR600829-4};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600829-4};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR600829-3};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001946};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600829-1"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600829-2"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600829-3"
FT   BINDING         76
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600829-4"
FT   BINDING         94..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600829-3"
SQ   SEQUENCE   127 AA;  13778 MW;  4D356A9B1C078606 CRC64;
     MGQYHKKPSN WESFGDAFQG ILYNCKTQRH FRFHVFTAAL VLLIAVWLRL ERWEWVVLLL
     TIGSVMAAEA FNTAVEIAVD LAEPDFNPQA GLAKDVAAGA VLITAIIAVA VGVVIFGPRL
     AGLLGLG
//