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Database: UniProt
Entry: B1IBK2_STRPI
LinkDB: B1IBK2_STRPI
Original site: B1IBK2_STRPI 
ID   B1IBK2_STRPI            Unreviewed;       294 AA.
AC   B1IBK2;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   OrderedLocusNames=SPH_1146 {ECO:0000313|EMBL:ACA36121.1};
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA36121.1, ECO:0000313|Proteomes:UP000002163};
RN   [1] {ECO:0000313|Proteomes:UP000002163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA36121.1; -; Genomic_DNA.
DR   RefSeq; WP_000710115.1; NC_010380.1.
DR   AlphaFoldDB; B1IBK2; -.
DR   SMR; B1IBK2; -.
DR   GeneID; 66806168; -.
DR   KEGG; spv:SPH_1146; -.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   Proteomes; UP000002163; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..131
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
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
//
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