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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//