YEGS_SHISS
ID YEGS_SHISS Reviewed; 299 AA.
AC Q3Z0C0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SSON_2136;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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; CP000038; AAZ88792.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z0C0; -.
DR SMR; Q3Z0C0; -.
DR EnsemblBacteria; AAZ88792; AAZ88792; SSON_2136.
DR KEGG; ssn:SSON_2136; -.
DR HOGENOM; CLU_045532_1_1_6; -.
DR OMA; GFDSRVN; -.
DR Proteomes; UP000002529; 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_0000292162"
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; 31946 MW; ADB730B209CEB51E CRC64;
MAEFPASLLI LNGKSTDNLP LREAIMLLRE EGMTIHVRVT WEKGDAARYV EEARKLGVAT
VIAGGGDGTI NEVSTALIQC EGDGIPALGI LPLGTANDFA TSVGIPEALD KALKLAIAGN
AIAIDMAQVN KQTCFINMAT GGFGTRITTE TPEKLKAALG GVSYIIHGLM RMDTLQPDRC
EIRGENFHWQ GDALVIGIGN GRQAGGGQQL CPNALINDGL LQLRIFTGDE ILPALVSTLK
SDEDNPNIIE GASSWFDIQA PHEITFNLDG EPLSGQNFHI EILPAALRCR LPPDCLLLR
