ID   YEGS_CHRSD              Reviewed;         311 AA.
AC   Q1QUK4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable lipid kinase YegS-like {ECO:0000255|HAMAP-Rule:MF_01377};
DE            EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_01377};
GN   OrderedLocusNames=Csal_2507;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- FUNCTION: Probably phosphorylates lipids; the in vivo substrate is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_01377}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01377};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01377};
CC       Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC       {ECO:0000255|HAMAP-Rule:MF_01377};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01377}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC       lipid kinase subfamily. {ECO:0000255|HAMAP-Rule:MF_01377}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000285; ABE59854.1; -; Genomic_DNA.
DR   RefSeq; WP_011507800.1; NC_007963.1.
DR   AlphaFoldDB; Q1QUK4; -.
DR   SMR; Q1QUK4; -.
DR   STRING; 290398.Csal_2507; -.
DR   EnsemblBacteria; ABE59854; ABE59854; Csal_2507.
DR   KEGG; csa:Csal_2507; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_1_6; -.
DR   OMA; GFDSRVN; -.
DR   OrthoDB; 869726at2; -.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001727; F:lipid kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   HAMAP; MF_01377; YegS; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR022433; Lip_kinase_YegS.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   TIGRFAMs; TIGR00147; TIGR00147; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..311
FT                   /note="Probable lipid kinase YegS-like"
FT                   /id="PRO_0000292140"
FT   DOMAIN          9..140
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         73..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
SQ   SEQUENCE   311 AA;  33336 MW;  ED1F1D2154CE9AEB CRC64;
     MNETIQPCEH DGDTWLILNG KSAQLPEVRE AVGRVREAGH HLAVRVTWEG GDGVRLAREA
     SEAGIARVIA GGGDGTVNEI VGGLMQLASE TRPALGILPL GSANDFAGGL GLPEEPYEAL
     RVALETPPRR VDVGTLGDDY FINLASGGFG AQITNSTPAP LKRLLGGGAY SLMGMLKAWN
     YQPYQGRLRF PDGERNVPLF LLALGNGCQA GGGQQLAPLA KIDDGLLELL IVRHFTSLRE
     MKQLIDELEN LPESGDFVEY LQVPWVEFES EHALPLNLDG EPCFHENFRA ALMPGALCLA
     APEGSALLSH Q