ID A0A0R2CZI5_9LACO Unreviewed; 296 AA.
AC A0A0R2CZI5;
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=Diacylglycerol kinase family lipid kinase {ECO:0000313|EMBL:KRM93513.1};
GN ORFNames=FC56_GL000225 {ECO:0000313|EMBL:KRM93513.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93513.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM93513.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93513.1,
RC ECO:0000313|Proteomes:UP000051256};
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:KRM93513.1}.
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DR EMBL; AYZR01000008; KRM93513.1; -; Genomic_DNA.
DR RefSeq; WP_056978130.1; NZ_AYZR01000008.1.
DR AlphaFoldDB; A0A0R2CZI5; -.
DR STRING; 1423802.FC56_GL000225; -.
DR PATRIC; fig|1423802.4.peg.227; -.
DR Proteomes; UP000051256; 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, ECO:0000313|EMBL:KRM93513.1};
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:UP000051256};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..129
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 296 AA; 32784 MW; 5E71170C7B2B6B78 CRC64;
MKYTVLYNQS AGDSDSEKRA KQFKNTAENA QQTVELIGTT SREQAIDYVQ KNIKNIETLV
VVGGDGSLNT VFSALISLDN SPVIGILPGG TVNNFARAMN IPLDSKAATE VILHGRVVNA
DLLHTNQRAI VSSLTLGTIA EMAKGVRQEE KQRWGALAYL FSGAKKILTT KPASIVVKSN
HQRYQFSTRF LLVTTTSSIG GFTKFDPEVD IDDHQIHITV LKRFSPWRLV GYFSYFITGQ
IRKLNDASYL KLEQANISSL DNKKVEVRID GDEAGELPVN LHVKKQFIKI IVPESD
//
