YEGS_PSEAE
ID YEGS_PSEAE Reviewed; 302 AA.
AC Q9HZI3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PA3023;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06411.1; -; Genomic_DNA.
DR PIR; D83268; D83268.
DR RefSeq; NP_251713.1; NC_002516.2.
DR RefSeq; WP_003091230.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q9HZI3; -.
DR SMR; Q9HZI3; -.
DR STRING; 287.DR97_4914; -.
DR PaxDb; Q9HZI3; -.
DR PRIDE; Q9HZI3; -.
DR EnsemblBacteria; AAG06411; AAG06411; PA3023.
DR GeneID; 882986; -.
DR KEGG; pae:PA3023; -.
DR PATRIC; fig|208964.12.peg.3172; -.
DR PseudoCAP; PA3023; -.
DR HOGENOM; CLU_045532_1_1_6; -.
DR InParanoid; Q9HZI3; -.
DR OMA; GFDSRVN; -.
DR PhylomeDB; Q9HZI3; -.
DR BioCyc; PAER208964:G1FZ6-3075-MON; -.
DR Proteomes; UP000002438; 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..302
FT /note="Probable lipid kinase YegS-like"
FT /id="PRO_0000292147"
FT DOMAIN 1..129
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 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 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01377"
FT BINDING 213
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"
SQ SEQUENCE 302 AA; 31505 MW; DBD61C20AC3B7343 CRC64;
MDKDKVLLVL HGKQAGNEEV RAAVAAQREA GRELAVRVTW EDGDARRIVE EALAAGYATL
VAGGGDGTLR EVAEALARGR GEASLAILPL GTANDFARAA GIPLEPAAAL ALLDQTARPI
DLGEVNGKLF LNMATGGFGS KVTANTSEDL KKVLGGAAYL LTGLTRFSEV HAAQGRFSAP
DFQWEGEFLA LGIGNGRQAG GGHVLCPQAR VDDGLLDVSI LPTPQDMVGT LGTLLGGGNG
VESLFVRARV PWLEVEAAEG LDVNLDGEPL EGRKLRFSVS PGALRVHLPA GSPLLREPPR
ED
