ID   YEGS_SALCH              Reviewed;         299 AA.
AC   Q57MK0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable lipid kinase YegS {ECO:0000255|HAMAP-Rule:MF_01377};
DE            EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_01377};
GN   Name=yegS {ECO:0000255|HAMAP-Rule:MF_01377}; OrderedLocusNames=SCH_2155;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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}.
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DR   EMBL; AE017220; AAX66061.1; -; Genomic_DNA.
DR   RefSeq; WP_001273389.1; NC_006905.1.
DR   AlphaFoldDB; Q57MK0; -.
DR   SMR; Q57MK0; -.
DR   EnsemblBacteria; AAX66061; AAX66061; SCH_2155.
DR   KEGG; sec:SCH_2155; -.
DR   HOGENOM; CLU_045532_1_1_6; -.
DR   OMA; GFDSRVN; -.
DR   Proteomes; UP000000538; 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; TIGR03702; lip_kinase_YegS; 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; Transferase.
FT   CHAIN           1..299
FT                   /note="Probable lipid kinase YegS"
FT                   /id="PRO_0000292155"
FT   DOMAIN          2..133
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   ACT_SITE        271
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         66..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
SQ   SEQUENCE   299 AA;  32029 MW;  4026FEFD5F2F0197 CRC64;
     MANFPASLLI LNGKSADNQP LREAITLLRD EGIQIHVRVT WEKGDAQRYV DEARRLGVET
     VIAGGGDGTI NEVSTALIQI RDGVAPALGL LPLGTANDFA TSAGIPEALD KALKLAIAGN
     AMEIDMAMVN DKTCFINMAT GGFGTRITTE TPEKLKAALG GVSYLIHGLM RMDTLTPDRC
     EIRGENFHWQ GDALVIGIGN GRQAGGGQQL CPTALINDGL LQLRIFTGEE LLPALFSTLT
     QSDDNPNIID GASAWFDIHA PHEITFNLDG EPLSGQEFHI EVLPGALRCR LPPDCPLLR