ID C4L688_EXISA Unreviewed; 332 AA.
AC C4L688;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Diacylglycerol kinase catalytic region {ECO:0000313|EMBL:ACQ69919.1};
GN OrderedLocusNames=EAT1b_0991 {ECO:0000313|EMBL:ACQ69919.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ69919.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ69919.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ69919.1; -; Genomic_DNA.
DR RefSeq; WP_012727038.1; NC_012673.1.
DR AlphaFoldDB; C4L688; -.
DR STRING; 360911.EAT1b_0991; -.
DR KEGG; eat:EAT1b_0991; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000000716; Chromosome.
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:ACQ69919.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 332 AA; 36849 MW; 33D5CC455EF2A614 CRC64;
MQRKRARVIY NPTSGKEVIK RELPYILNRL EDAGYETSTY ATKAIGDATL EAKRASAAEF
DLIIAAGGDG TLNEVISGLA PLENRPTIGL IPVGTTNDFA RAMRIPLSVV GALDVICDGF
EMPVDLGEIE GEKGDIHYFI NIAGGGIMTE LSYEVPSKLK TALGQLAYYV KGMEKLPLIK
PTYIELEHDE GTFQGEVMVF LTSNSNSVGG FEKISPHASL NDGLFDLFIL RKCNLFEFIH
VVRLLLRGEH LSSSLVEHVK TSRVRMKTTE PMSLNIDGEY GGECTGEMRN LFRHLTVLAP
NARIREMEDL NAQYEREQMI KQLFNVSLDK AE
//
