ID A0A0R2DWA8_9LACO Unreviewed; 305 AA.
AC A0A0R2DWA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lipid kinase YegS {ECO:0000313|EMBL:KRN04468.1};
GN ORFNames=FC86_GL000145 {ECO:0000313|EMBL:KRN04468.1};
OS Holzapfeliella floricola DSM 23037 = JCM 16512.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Holzapfeliella.
OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04468.1, ECO:0000313|Proteomes:UP000051378};
RN [1] {ECO:0000313|EMBL:KRN04468.1, ECO:0000313|Proteomes:UP000051378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04468.1,
RC ECO:0000313|Proteomes:UP000051378};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN04468.1}.
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DR EMBL; AYZL01000010; KRN04468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2DWA8; -.
DR STRING; 1423744.FC86_GL000145; -.
DR PATRIC; fig|1423744.4.peg.149; -.
DR Proteomes; UP000051378; 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:KRN04468.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051378};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..134
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 305 AA; 33404 MW; 081DA5C88831DC75 CRC64;
MPKARLIYNP TSGHYPVTKS VVDILKVLED AGFEASSFQT TVEVDSAKNE ATRAAKAGFD
LIVSAGGDGT LDQVINGIAP LVTRPKVAVI PAGTANDFAR ALNIPRNNFK EAAEVILKGQ
TQKLDIGRAY SSTNSQYFVN NAGGGHVTEV TYAPTWQQKS IFGYSAYLLN AIKLLAGLQS
RKMRLTYDTG VYEGETVLFL LGLTNSIGGF EKILPIPEFS DGNFGLLIVK PTQLNRLFRL
IKLAVKNRQH LTDDDVIFVK TKTLEVELLD QNSHGNDVNI DGEKGTAFPL SFENLTQHIE
FYVNF
//
