ID   YEGS_YERP3              Reviewed;         296 AA.
AC   A7FG10;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=YpsIP31758_1207;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49604.1; -; Genomic_DNA.
DR   RefSeq; WP_002209799.1; NC_009708.1.
DR   AlphaFoldDB; A7FG10; -.
DR   SMR; A7FG10; -.
DR   EnsemblBacteria; ABS49604; ABS49604; YpsIP31758_1207.
DR   GeneID; 57975813; -.
DR   KEGG; ypi:YpsIP31758_1207; -.
DR   HOGENOM; CLU_045532_1_1_6; -.
DR   OMA; GFDSRVN; -.
DR   Proteomes; UP000002412; 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..296
FT                   /note="Probable lipid kinase YegS-like"
FT                   /id="PRO_1000068256"
FT   DOMAIN          1..130
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         63..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
SQ   SEQUENCE   296 AA;  31535 MW;  E3D5719B9F884A73 CRC64;
     MPHTLLILNG KESGNPEVRE AVKNVRDEGL TLHVRITWEH GDAKRYVEEA ATLAVSTVIA
     GGGDGTINEV ATALMSLPAD KRPCLGILPL GTANDFATGC NIPLQIENAL QLAVKGRAVA
     IDLAQVNGEH YFINMATGGF GTRITTETPD KLKAALGGVS YFIHGLMRLD ALKADSCKIH
     GPDFHWSGDA LVIGIGNGKQ AGGGQLLCPD ALINDGLMQL RLLTAKELLP AVLSTLFNGE
     KNKNVIDATV PWLDITAPND ITFNLDGEPL SGRHFHIEIL PHAIQCRLPP NCPLLG