YEGS_ECOLI
ID YEGS_ECOLI Reviewed; 299 AA.
AC P76407; O08008; O08011;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lipid kinase YegS;
DE EC=2.7.1.-;
GN Name=yegS; OrderedLocusNames=b2086, JW2070;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=K12;
RX PubMed=16511327; DOI=10.1107/s1744309106004799;
RA Bakali H.M.A., Nordlund P., Hallberg B.M.;
RT "Expression, purification, crystallization and preliminary diffraction
RT studies of the mammalian DAG kinase homologue yegS from Escherichia coli.";
RL Acta Crystallogr. F 62:295-297(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH ADP
RP AND MAGNESIUM, CHARACTERIZATION, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=17351295; DOI=10.1074/jbc.m604852200;
RA Bakali H.M.A., Herman M.D., Johnson K.A., Kelly A.A., Wieslander A.,
RA Hallberg B.M., Nordlund P.;
RT "Crystal structure of yegS, a homologue to the mammalian diacylglycerol
RT kinases, reveals a novel regulatory metal binding site.";
RL J. Biol. Chem. 282:19644-19652(2007).
CC -!- FUNCTION: In vitro phosphorylates phosphatidylglycerol but not
CC diacylglycerol; the in vivo substrate is unknown.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17351295};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17351295};
CC Note=Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
CC {ECO:0000269|PubMed:17351295};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for phosphatidylglycerol;
CC Vmax=29.7 nmol/min/mg enzyme;
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 5 to 9.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16511327,
CC ECO:0000269|PubMed:17351295}.
CC -!- INTERACTION:
CC P76407; P0ABH7: gltA; NbExp=3; IntAct=EBI-1127478, EBI-547808;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17351295}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS
CC lipid kinase subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC75147.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15939.1; -; Genomic_DNA.
DR PIR; E64975; E64975.
DR RefSeq; NP_416590.1; NC_000913.3.
DR RefSeq; WP_000807348.1; NZ_LN832404.1.
DR PDB; 2BON; X-ray; 1.90 A; A/B=1-299.
DR PDB; 2JGR; X-ray; 2.65 A; A=1-299.
DR PDBsum; 2BON; -.
DR PDBsum; 2JGR; -.
DR AlphaFoldDB; P76407; -.
DR SMR; P76407; -.
DR BioGRID; 4261758; 16.
DR BioGRID; 850972; 3.
DR DIP; DIP-11889N; -.
DR IntAct; P76407; 8.
DR STRING; 511145.b2086; -.
DR jPOST; P76407; -.
DR PaxDb; P76407; -.
DR PRIDE; P76407; -.
DR EnsemblBacteria; AAC75147; AAC75147; b2086.
DR EnsemblBacteria; BAA15939; BAA15939; BAA15939.
DR GeneID; 946626; -.
DR KEGG; ecj:JW2070; -.
DR KEGG; eco:b2086; -.
DR PATRIC; fig|511145.12.peg.2163; -.
DR EchoBASE; EB4111; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_1_6; -.
DR InParanoid; P76407; -.
DR OMA; GFDSRVN; -.
DR PhylomeDB; P76407; -.
DR BioCyc; EcoCyc:G7123-MON; -.
DR BioCyc; MetaCyc:G7123-MON; -.
DR EvolutionaryTrace; P76407; -.
DR PRO; PR:P76407; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
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 DisProt; DP01981; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..299
FT /note="Lipid kinase YegS"
FT /id="PRO_0000169129"
FT DOMAIN 2..133
FT /note="DAGKc"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 66..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17351295"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17351295"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17351295"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:2BON"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:2BON"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2JGR"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 187..202
FT /evidence="ECO:0007829|PDB:2BON"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2JGR"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2BON"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 248..268
FT /evidence="ECO:0007829|PDB:2BON"
FT STRAND 271..291
FT /evidence="ECO:0007829|PDB:2BON"
SQ SEQUENCE 299 AA; 32039 MW; 4C90DDD8456C2829 CRC64;
MAEFPASLLI LNGKSTDNLP LREAIMLLRE EGMTIHVRVT WEKGDAARYV EEARKFGVAT
VIAGGGDGTI NEVSTALIQC EGDDIPALGI LPLGTANDFA TSVGIPEALD KALKLAIAGD
AIAIDMAQVN KQTCFINMAT GGFGTRITTE TPEKLKAALG SVSYIIHGLM RMDTLQPDRC
EIRGENFHWQ GDALVIGIGN GRQAGGGQQL CPNALINDGL LQLRIFTGDE ILPALVSTLK
SDEDNPNIIE GASSWFDIQA PHDITFNLDG EPLSGQNFHI EILPAALRCR LPPDCPLLR
