ID C4L162_EXISA Unreviewed; 290 AA.
AC C4L162;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Diacylglycerol kinase catalytic region {ECO:0000313|EMBL:ACQ69008.1};
GN OrderedLocusNames=EAT1b_0074 {ECO:0000313|EMBL:ACQ69008.1};
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:ACQ69008.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ69008.1, 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; ACQ69008.1; -; Genomic_DNA.
DR RefSeq; WP_012726127.1; NC_012673.1.
DR AlphaFoldDB; C4L162; -.
DR STRING; 360911.EAT1b_0074; -.
DR KEGG; eat:EAT1b_0074; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_1_9; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; 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 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 SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ACQ69008.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:ACQ69008.1}.
FT DOMAIN 1..128
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 290 AA; 32104 MW; D7D1A977257EA4B9 CRC64;
MRALIISNPK SGTSETMLGE VIGTIESLYE EIIIKKTQEI GDALRFAETS ESFDHLIVIG
GDGTLNEVVN GLMTLQREER PTVGIIPAGT CNDFARALEL PIQPTQAAQI IRSSHEQHVD
VIQVDEMYAL NFVGVGLIAD TSRQIDPDEK ESLGSIGYFL ATIRQFREAD PFNITLRRGS
EVIYDGDVSF LYVGNGSYLG TVPTKLETQS FSDGLLEVVH SSAIGFPMIR QLLAQQLGLD
QKSTEWNHFQ ASHIELELNA PQIIDVDGEH FEADKLSIRI RERALTFLTP
//
