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Database: UniProt
Entry: T1ZE03_STRIT
LinkDB: T1ZE03_STRIT
Original site: T1ZE03_STRIT 
ID   T1ZE03_STRIT            Unreviewed;       319 AA.
AC   T1ZE03;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative lipid kinase {ECO:0000313|EMBL:AGU76110.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:AGU76110.1};
GN   ORFNames=SIR_0742 {ECO:0000313|EMBL:AGU76110.1};
OS   Streptococcus intermedius B196.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU76110.1, ECO:0000313|Proteomes:UP000016233};
RN   [1] {ECO:0000313|EMBL:AGU76110.1, ECO:0000313|Proteomes:UP000016233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B196 {ECO:0000313|EMBL:AGU76110.1,
RC   ECO:0000313|Proteomes:UP000016233};
RX   PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA   Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA   Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA   Corbett C.R.;
RT   "Phylogenetic relationship and virulence inference of Streptococcus
RT   Anginosus Group: curated annotation and whole-genome comparative analysis
RT   support distinct species designation.";
RL   BMC Genomics 14:895-895(2013).
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; CP003857; AGU76110.1; -; Genomic_DNA.
DR   RefSeq; WP_003076850.1; NZ_UZBH01000001.1.
DR   AlphaFoldDB; T1ZE03; -.
DR   GeneID; 57844807; -.
DR   KEGG; sib:SIR_0742; -.
DR   PATRIC; fig|862967.3.peg.743; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000016233; 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:AGU76110.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGU76110.1}.
FT   DOMAIN          3..137
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   319 AA;  34740 MW;  359EA86F65EBF798 CRC64;
     METARKRARL IYNPTSGQEI IKKNIAEVLD VLEDVGYETS AYQTTPAPLS AQNEAERAAK
     AGFDLIVAAG GDGTINEVVN GVAPLENRPK LAFIPTGTTN DYARALKIPM GDPVAAARII
     EKDQTIKMDI GQAYGKKYFI NIAAAGTLTE LTYSVPSEVK SRLGYLAYVA KGAEMLPKSK
     LRKVHIEHDH GVFEGKVSLI FAALTNSIGG FEKLAPDTVL DDGNFTLILV KTARLFDMLA
     LMIQAINGGQ HVTDANVEYL KTSKLKLEVL DKKAPFMLNL DGEYGGDTPV ELEVLHNHLE
     FFANIDEISD SALSLENRE
//
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