ID A0A0R1LNX0_9LACO Unreviewed; 339 AA.
AC A0A0R1LNX0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Lipid kinase {ECO:0000313|EMBL:KRK97192.1};
GN ORFNames=FD04_GL002054 {ECO:0000313|EMBL:KRK97192.1};
OS Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK97192.1, ECO:0000313|Proteomes:UP000051160};
RN [1] {ECO:0000313|EMBL:KRK97192.1, ECO:0000313|Proteomes:UP000051160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK97192.1,
RC ECO:0000313|Proteomes:UP000051160};
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:KRK97192.1}.
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DR EMBL; AZEE01000030; KRK97192.1; -; Genomic_DNA.
DR RefSeq; WP_056948975.1; NZ_AZEE01000030.1.
DR AlphaFoldDB; A0A0R1LNX0; -.
DR STRING; 1423776.FD04_GL002054; -.
DR PATRIC; fig|1423776.4.peg.2080; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000051160; 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:KRK97192.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..134
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 339 AA; 37168 MW; 450F9A0B7255FBCF CRC64;
MRKRARVIYN PSSGREALKK DMVDILGVFE QAGYETSAFA TTPAPNSARD EAERAGRDGF
DLVVAAGGDG TINEVVNGLA GLKKRPKMAI IPAGTTNDYA RALRIPREDP LAAAKVVLKN
QTIKMDIGLA GKNYFVNIAG GGRLTELTYE VPSNLKTLFG YLAYLVKGAE LLPRIRPFKM
DLKFDGDEYV GDASMFFLAL TNSVGGFEQI VPDASLNDGM FTMIIVKTSN LAEILHLLTL
VLNGGRHIND PRIIYRKVRK VDVKSLDDSR IMINLDGEYG GDAPMNFTNL KQHIETYANL
DDIPDAAVET EDPELLEAER KFLAGVHELP EDQSSTQSK
//
