ID A0A160ISA2_9BACI Unreviewed; 301 AA.
AC A0A160ISA2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:MQR95941.1};
DE SubName: Full=Lipid kinase {ECO:0000313|EMBL:ANC79227.1};
GN ORFNames=ABE65_001555 {ECO:0000313|EMBL:ANC79227.1}, EJV22_12165
GN {ECO:0000313|EMBL:MQR95941.1};
OS Fictibacillus phosphorivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC79227.1, ECO:0000313|Proteomes:UP000076623};
RN [1] {ECO:0000313|EMBL:ANC79227.1, ECO:0000313|Proteomes:UP000076623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC79227.1,
RC ECO:0000313|Proteomes:UP000076623};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT toxic to nematodes.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MQR95941.1, ECO:0000313|Proteomes:UP000366026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DBL 17U12 {ECO:0000313|EMBL:MQR95941.1,
RC ECO:0000313|Proteomes:UP000366026};
RA Shahi N., Mallik S.K., Rawat S.;
RT "Draft whole genome sequence of algicidal bacterium F. phosphorivorans.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP015378; ANC79227.1; -; Genomic_DNA.
DR EMBL; SAYN01000023; MQR95941.1; -; Genomic_DNA.
DR RefSeq; WP_066399616.1; NZ_SAYN01000023.1.
DR AlphaFoldDB; A0A160ISA2; -.
DR STRING; 1221500.ABE65_001555; -.
DR KEGG; fpn:ABE65_001555; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000076623; Chromosome.
DR Proteomes; UP000366026; 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:ANC79227.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..132
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 301 AA; 33132 MW; EB6AEB633F1AD523 CRC64;
MKRARLIYNP SSGRETVKKQ LPYILNRLEN AGYETSCHAT TPEDGCATRA ARAAGERGFD
LVIAAGGDGT IYEVVNGLAG LENRPMLGII PAGTTNDFAR AVGVPRTIEG ACDVLCGGVH
MPVDIGKVND KFFINIAGGG RITELTYEVP SKLKTMIGQL AYFLKGIEML PSIRPTFVEI
EFDDKEKYEG EIMLFLVANT NSVGGFEKLA PSSEFHDGLF DVIILKKTNL AEFVRIASLA
IRGEHIHDDH VIYKKAKRVK VTPREKMQIN LDGELGGILP GEFENLHHHF ELLVPKERLK
P
//