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Database: UniProt
Entry: G5KF00_9STRE
LinkDB: G5KF00_9STRE
Original site: G5KF00_9STRE 
ID   G5KF00_9STRE            Unreviewed;       340 AA.
AC   G5KF00;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Putative lipid kinase {ECO:0000313|EMBL:EHJ56094.1};
GN   ORFNames=STRUR_0904 {ECO:0000313|EMBL:EHJ56094.1};
OS   Streptococcus urinalis 2285-97.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ56094.1, ECO:0000313|Proteomes:UP000005388};
RN   [1] {ECO:0000313|EMBL:EHJ56094.1, ECO:0000313|Proteomes:UP000005388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2285-97 {ECO:0000313|EMBL:EHJ56094.1};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ56094.1}.
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DR   EMBL; AEUZ02000001; EHJ56094.1; -; Genomic_DNA.
DR   RefSeq; WP_006738865.1; NZ_AEUZ02000001.1.
DR   AlphaFoldDB; G5KF00; -.
DR   STRING; 764291.STRUR_0904; -.
DR   eggNOG; COG1597; Bacteria.
DR   Proteomes; UP000005388; Unassembled WGS sequence.
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:EHJ56094.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005388};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..136
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   340 AA;  37442 MW;  BD6C3DE0DD5C005B CRC64;
     MKKQLKARLI YNPTSGQEIM KKNVAEVLNI LESYGYETSA FQTTPEENSA KNEAARAAKA
     GFDLVIAAGG DGTINEVVNG IAPLPKRPKM AIIPTGTTND FARALKIPRG NPIEAAKIIG
     KNQVIAMDIG RAYEKTYFIN IAAAGSLTEL TYSVPSQLKT MFGYLAYLAK GVELLPRIKN
     VPLKITHDNG VFEGKVSMIF AAITNSVGGF EQIAPDAKLD DGLFTLILVK TANLFEIVHL
     IRLVLDGGKH INDRRIEYIK TSKIEIEPKS KQRMMINLDG EYGGDAPVKL ENFKNHIRFF
     ADTDEISDDA LVLDTEDLAL EAIAQKFTHE VEDLDQNLEE
//
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