ID B8L803_9GAMM Unreviewed; 317 AA.
AC B8L803;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Probable lipid kinase YegS-like {ECO:0000256|HAMAP-Rule:MF_01377};
DE EC=2.7.1.- {ECO:0000256|HAMAP-Rule:MF_01377};
GN ORFNames=SSKA14_2395 {ECO:0000313|EMBL:EED39378.1};
OS Stenotrophomonas sp. SKA14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=391601 {ECO:0000313|EMBL:EED39378.1};
RN [1] {ECO:0000313|EMBL:EED39378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA14 {ECO:0000313|EMBL:EED39378.1};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (DEC-2008) 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}.
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DR EMBL; DS999412; EED39378.1; -; Genomic_DNA.
DR RefSeq; WP_008266759.1; NZ_DS999412.1.
DR AlphaFoldDB; B8L803; -.
DR HOGENOM; CLU_045532_1_1_6; -.
DR Proteomes; UP000003991; 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 1..134
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 65..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01377"
SQ SEQUENCE 317 AA; 33349 MW; F32950524A9CEE33 CRC64;
MTIPRWRLIL NGKSAGNDEL RDAVGHWRGQ GVQLDVRVTW EDGDAERYVA EAIDHGVDVI
VAAGGDGTLS AVAETLAHRE EPADALPSLA LIPMGTANDF ATSAGIPTEP KDAFALIGQA
PPHAIDLLRV DADGTPWWCA NLASGGFGTQ VTVETDAGLK KMLGGLAYVI TGIAKLGRIE
PIRARLSGPD FAWEGDFIAL GIGNGRQAGG GQQLCPQALI DDGLLDVTVL PELEGEVTTT
LGQMLKSGTQ AALEQLATRA RLPWLQIASE RPLTLNLDGE PVQARQFRIE CVPGRVRMHL
PAGCPLLGGV SGLDVGP
//
