Y1045_STRPN
ID Y1045_STRPN Reviewed; 294 AA.
AC Q97QZ6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative lipid kinase SP_1045;
DE EC=2.7.1.-;
GN OrderedLocusNames=SP_1045;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP LACK OF FUNCTION AS A DIACYLGLYCEROL KINASE.
RX PubMed=17535816; DOI=10.1074/jbc.m703536200;
RA Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT "Identification of a soluble diacylglycerol kinase required for
RT lipoteichoic acid production in Bacillus subtilis.";
RL J. Biol. Chem. 282:21738-21745(2007).
CC -!- FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids
CC other than diacylglycerol (DAG). In fact, is not able to exhibit
CC diacylglycerol kinase activity in vitro.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC structural role and is required for catalytic activity. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
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DR EMBL; AE005672; AAK75160.1; -; Genomic_DNA.
DR PIR; G95120; G95120.
DR RefSeq; WP_000710115.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97QZ6; -.
DR SMR; Q97QZ6; -.
DR STRING; 170187.SP_1045; -.
DR DNASU; 931559; -.
DR EnsemblBacteria; AAK75160; AAK75160; SP_1045.
DR GeneID; 66806168; -.
DR KEGG; spn:SP_1045; -.
DR eggNOG; COG1597; Bacteria.
DR OMA; VNDAYFM; -.
DR PhylomeDB; Q97QZ6; -.
DR BioCyc; SPNE170187:G1FZB-1074-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10330; -; 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 Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..294
FT /note="Putative lipid kinase SP_1045"
FT /id="PRO_0000386523"
FT DOMAIN 1..131
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 9..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 66..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 32682 MW; 9479844B578CEDB3 CRC64;
MKKAMVIINP TSGGEKALDY KEKLENKAKE YFEYVETKIT EKALDATHFA EEASREQYDA
VVVFGGDGTV NEVISGIDER DYIPKLGIIP GGTGNLITKL LEINQDIDGA IDELDFDLTN
KIDIGKANDN YFGYIFSIGS LPEAIHNVEI EDKTKFGILT YAVNTMKSVM TDQVFNIKVE
TENGNYVGEA SHVLVLLTNY FADKKIFEEN KDGYANILIL KDASIFSKLS VIPDLLKGDV
VANDNIEYIK ARNIKISSDS ELESDVDGDK SDNLPVEIKV LAQRVEVFSK PKED
