ID W1SE51_9BACI Unreviewed; 313 AA.
AC W1SE51;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative lipid kinase {ECO:0000313|EMBL:ETI67457.1};
GN ORFNames=BAVI_17582 {ECO:0000313|EMBL:ETI67457.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67457.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI67457.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67457.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(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}.
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:ETI67457.1}.
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DR EMBL; ALAN01000095; ETI67457.1; -; Genomic_DNA.
DR RefSeq; WP_024029694.1; NZ_ALAN01000095.1.
DR AlphaFoldDB; W1SE51; -.
DR STRING; 220686.AA980_06575; -.
DR PATRIC; fig|1131730.3.peg.3694; -.
DR eggNOG; COG1597; Bacteria.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:ETI67457.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..131
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 313 AA; 34636 MW; 240493B8A6D54AA8 CRC64;
MKRARLIYNP TSGREMIKRH LPEILQKLEA AGYEASCHAT TGAGDATKAA QIAVKRKYDI
VIAAGGDGTI HEVVNGLADQ EYRPKLGIIP TGTTNDFARA LHIPRDVSTA VNIITKGEMI
PVDIGRINDK YFINIAGGGR ITELTYEVPS KLKTMLGQLA YYLKGMEMLP SIKASHLRIE
YDGKLFEGEA MMFLVGLTNS IGGFERLAPD ASINDGLFSL LILKKVNLAE FIRIATLAVR
GEHVNDQNVI YTQANRIKVY SSEKVQLNLD GEFGGLLPAE FENLYRHLEV FVPLADIRPN
DRPTNWQSGK KYS
//
