ID A0A108UCT2_9GAMM Unreviewed; 325 AA.
AC A0A108UCT2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AZ78_4096 {ECO:0000313|EMBL:KWS06540.1};
OS Lysobacter capsici AZ78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS06540.1, ECO:0000313|Proteomes:UP000023435};
RN [1] {ECO:0000313|EMBL:KWS06540.1, ECO:0000313|Proteomes:UP000023435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS06540.1,
RC ECO:0000313|Proteomes:UP000023435};
RX PubMed=24762937;
RA Puopolo G., Sonego P., Engelen K., Pertot I.;
RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT to Plant-Pathogenic Oomycetes.";
RL Genome Announc. 2:0-0(2014).
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:KWS06540.1}.
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DR EMBL; JAJA02000001; KWS06540.1; -; Genomic_DNA.
DR RefSeq; WP_051547120.1; NZ_JAJA02000001.1.
DR AlphaFoldDB; A0A108UCT2; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000023435; 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 325 AA; 33992 MW; 76BCB8ACBC8724B0 CRC64;
MPKPRWRLIL NGKSAGDDAL REAVGAIRDR GIVLDVRVTW ESGDAERYVS EAIADGVATI
IAAGGDGTLS EVATTLAHRD ESADVLPSLG LVPLGTANDF ASAALIPTDP AQALDLIDRQ
APRPIDLIRL EAPDGLHWAA NLASGGFGTQ VTIETDAGLK KMLGGLAYLV TGISKLGKIE
PMRARLHGDG FEWEGDFIAL GIGNGKQAGG GQALCPDALI DDGLLDVTVV PELSGEVGAT
VRTLLTEGKH AALDRVAARA QLKYVEIDSP QGLTLNLDGE PVHAHHFRID CVPARLRMHL
PADCPLLSAS AAQALPGALA TESDR
//
