ID W1EY15_ECOLX Unreviewed; 299 AA.
AC W1EY15;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Probable lipid kinase YegS {ECO:0000256|HAMAP-Rule:MF_01377};
DE EC=2.7.1.- {ECO:0000256|HAMAP-Rule:MF_01377};
GN Name=yegS {ECO:0000256|HAMAP-Rule:MF_01377};
OS Escherichia coli ISC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL25677.1, ECO:0000313|Proteomes:UP000019199};
RN [1] {ECO:0000313|EMBL:CDL25677.1, ECO:0000313|Proteomes:UP000019199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISC7 {ECO:0000313|EMBL:CDL25677.1,
RC ECO:0000313|Proteomes:UP000019199};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably phosphorylates lipids; the in vivo substrate is
CC unknown. {ECO:0000256|HAMAP-Rule:MF_01377}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01377};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01377};
CC Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC {ECO:0000256|HAMAP-Rule:MF_01377};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01377}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC lipid kinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01377}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL25677.1}.
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DR EMBL; CBWN010000040; CDL25677.1; -; Genomic_DNA.
DR AlphaFoldDB; W1EY15; -.
DR SMR; W1EY15; -.
DR Proteomes; UP000019199; Unassembled WGS sequence.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 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 NCBIfam; TIGR03702; lip_kinase_YegS; 1.
DR NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01377}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01377};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01377};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01377};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01377};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01377};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01377};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01377};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01377}.
FT DOMAIN 2..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 66..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
SQ SEQUENCE 299 AA; 31988 MW; FC4A1C427832552F CRC64;
MAEFPASLLI LNGKSTDNLP LREAIMLLRE EGMTIHVRVT WEKGDAARYV EEARKLGVAT
VIAGGGDGTI NEVSTALIQC EGDDIPALGI LPLGTANDFA TSVGIPEALD KALKLAIAGN
AIAIDMAQVN KQTCFINMAT GGFGTRITTE TPEKLKAALG GVSYIIHGLM RMDTLQPDRC
EIRGENFHWQ GDALVIGIGN GRQAGGGQQL CPNALINDGL LQLRIFTGDE ILPALVSTLK
SDEDNPNIIE GASSWFDIQA PHEITFNLDG EPLSGQNFHI EILPAALRCR LPPDCPLLR
//
