ID A0A0R2G1W1_9LACO Unreviewed; 302 AA.
AC A0A0R2G1W1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=IV38_GL001645 {ECO:0000313|EMBL:KRN28192.1}, IV40_GL001570
GN {ECO:0000313|EMBL:KRN30932.1};
OS Lactobacillus selangorensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN30932.1, ECO:0000313|Proteomes:UP000051645};
RN [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN28192.1,
RC ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC {ECO:0000313|EMBL:KRN30932.1, ECO:0000313|Proteomes:UP000051645};
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:KRN30932.1}.
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DR EMBL; JQAT01000004; KRN28192.1; -; Genomic_DNA.
DR EMBL; JQAZ01000005; KRN30932.1; -; Genomic_DNA.
DR RefSeq; WP_057770066.1; NZ_JQAZ01000005.1.
DR AlphaFoldDB; A0A0R2G1W1; -.
DR STRING; 81857.IV38_GL001645; -.
DR PATRIC; fig|81857.3.peg.1656; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000051645; Unassembled WGS sequence.
DR Proteomes; UP000051751; 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:SF106; LIPID KINASE YEGS; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051645};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..133
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 302 AA; 33341 MW; 24A9D2B24435B858 CRC64;
MKTITVIYNP HSGHNRGGAI AQQFKEAAHQ LEPHTDVQLE AIRGKNDGRQ FAHQASLRQR
DLIVVVGGDG TINQVASGMV SVPHPPKLGI LPGGTVNNLA HVLHIPLDIP GAIATILGKH
SQPIDIGQIN RNHYMISTMT IGILADAALD VSQTEKQKFG PLAFVFKGIK VLAEHQHYQI
TLAGDHHFWQ KDTQLVLITM TNSVGGFTNF DPTAESDDGY FHVFLAPKMS YWRSLLFFPY
FITGNFSKIP GMTYLTMSHL TMTVTKNRHA VRTRIDGDPS VTLPLKMKVL KSALRVMTPE
PE
//
