ID   YEGS_STRMK              Reviewed;         309 AA.
AC   B2FKL6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Smlt4314;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ47699.1; -; Genomic_DNA.
DR   RefSeq; WP_012481442.1; NC_010943.1.
DR   AlphaFoldDB; B2FKL6; -.
DR   SMR; B2FKL6; -.
DR   STRING; 522373.Smlt4314; -.
DR   EnsemblBacteria; CAQ47699; CAQ47699; Smlt4314.
DR   KEGG; sml:Smlt4314; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_1_6; -.
DR   OMA; GFDSRVN; -.
DR   OrthoDB; 869726at2; -.
DR   Proteomes; UP000008840; 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; Reference proteome; Transferase.
FT   CHAIN           1..309
FT                   /note="Probable lipid kinase YegS-like"
FT                   /id="PRO_1000144880"
FT   DOMAIN          1..134
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   ACT_SITE        280
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         65..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT   BINDING         222
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"
SQ   SEQUENCE   309 AA;  32591 MW;  DE0DB54DA7193986 CRC64;
     MTTPRWRLIL NGKSAGNDEL RDAVGHWRGQ GVQLEVRVTW EDGDAERYVA EAIDHGVDVI
     VAAGGDGTLS AVAETLAHRE ELADALPSLA LIPMGTANDF ATAAGIPTEP KEAFALIGQA
     TPHAIDLLRV DADGTQWWCA NLASGGFGTQ VTVETDAGLK KMLGGLAYVI TGIAKLGRIE
     PITARLSGPD FAWEGDFIAL GIGNGRQAGG GQQLCPQALI DDGLLDVTVL PELEGEVTAT
     LGQMLKSGTQ AALEQLATRA RLPWLEIASE RPLTLNLDGE PVQARQFRIE CVPGRVRMHL
     PAGCPLLGG