ID V9W3E5_9BACL Unreviewed; 314 AA.
AC V9W3E5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Diacylglycerol kinase DagK {ECO:0000313|EMBL:AHD04673.1};
DE EC=2.7.1.107 {ECO:0000313|EMBL:AHD04673.1};
GN Name=dagK {ECO:0000313|EMBL:AHD04673.1};
GN ORFNames=ERIC2_c08400 {ECO:0000313|EMBL:AHD04673.1};
OS Paenibacillus larvae subsp. larvae DSM 25430.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD04673.1, ECO:0000313|Proteomes:UP000029431};
RN [1] {ECO:0000313|EMBL:AHD04673.1, ECO:0000313|Proteomes:UP000029431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD04673.1,
RC ECO:0000313|Proteomes:UP000029431};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000256|ARBA:ARBA00005983}.
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DR EMBL; CP003355; AHD04673.1; -; Genomic_DNA.
DR RefSeq; WP_024093395.1; NZ_CP019652.1.
DR AlphaFoldDB; V9W3E5; -.
DR GeneID; 64220423; -.
DR KEGG; plv:ERIC2_c08400; -.
DR PATRIC; fig|697284.3.peg.802; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR Proteomes; UP000029431; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR PANTHER; PTHR12358:SF115; DIACYLGLYCEROL KINASE; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AHD04673.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029431};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHD04673.1}.
FT DOMAIN 1..132
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 314 AA; 34597 MW; C548FB9A98D02CBA CRC64;
MTKRARLIYN PTSGREEMKR RLAEVLRRLE EGGLETSTHA TTGEGDATKA AAEAVDRGFD
VVIAAGGDGT LYEVINGLCG KPERPPLGIL PLGTTNDFAR ALGIPKNLEQ ACDIITEQFT
RDIDVGKVND RYYINIAAGG SFTELTYEVP SKLKTVLGQL AYYVKGLEKL PRLKPIHLDL
RCEEITIQED VMLFLITNSN SVGGFEKLAA DASLNDGLFD VIVLKKCNLA EFIRIATLAL
RGDHLADPNI VYFQTRELEI TSPDYVQLNL DGELGGTLPA VITNLQSHLK IFVDESGKST
YTKQLKQLGV RRRQ
//
