ID Q97L83_CLOAB Unreviewed; 295 AA.
AC Q97L83;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Unsharacterized protein, BmrU family {ECO:0000313|EMBL:AAK78656.1};
GN OrderedLocusNames=CA_C0679 {ECO:0000313|EMBL:AAK78656.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK78656.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK78656.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78656.1; -; Genomic_DNA.
DR PIR; E96983; E96983.
DR RefSeq; NP_347316.1; NC_003030.1.
DR RefSeq; WP_010963998.1; NC_003030.1.
DR AlphaFoldDB; Q97L83; -.
DR STRING; 272562.CA_C0679; -.
DR GeneID; 44997190; -.
DR KEGG; cac:CA_C0679; -.
DR PATRIC; fig|272562.8.peg.882; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000000814; 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: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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..130
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 295 AA; 32957 MW; 92148C143400C2D1 CRC64;
MNKVKFIYNP FSGENLIINN IDKVIKTHQK YGYTIVPHRI ELNCSIESAF DDIDDTYKYV
LIAGGDGTVD NVVNVMKKCN LDIPIAILPV GTANDFAKFI GMPADIEMAC EQILNSEIRK
IDIGKINDKY FINVASAGLF TNVSQKTDIN MKNTMGKLAY YVKGIEQLPN FKRIPLKVES
KQNNFDGEML LMLVFNGQTA GNFKFAYKAI VDDGMLDVII IEGGMVKDIV NILIKMFKGE
HLEDVNGIIY FKTDKLNISC NNDIVTDIDG ERGPDFPVEI TCIKGGLKIF GVKNI
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