ID   A0A6L8P1L2_BACAN        Unreviewed;       300 AA.
AC   A0A6L8P1L2; A0A1Q4M4T3; E9RA50; E9RA51; Q6HRT1; Q6KL39; Q81KC6;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=BmrU protein {ECO:0000313|EMBL:AAT34198.1};
GN   OrderedLocusNames=GBAA_5075 {ECO:0000313|EMBL:AAT34198.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT34198.1, ECO:0000313|Proteomes:UP000000594};
RN   [1] {ECO:0000313|EMBL:AAT34198.1, ECO:0000313|Proteomes:UP000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [2] {ECO:0007829|PDB:3S40}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RA   Tan K., Zhang R., Xu X., Cui H., Peterson S., Savchenko A., Anderson W.F.,
RA   Joachimiak A.;
RT   "The crystal structure of a diacylglycerol kinases from Bacillus anthracis
RT   str. Sterne.";
RL   Submitted (MAY-2011) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:3T5P}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Hou J., Zheng H., Chruszcz M., Cooper D.R., Onopriyenko O., Grimshaw S.,
RA   Savchenko A., Anderson W.F., Minor W.;
RT   "Crystal structure of a putative diacylglycerol kinase from Bacillus
RT   anthracis str. Sterne.";
RL   Submitted (JUL-2011) to the PDB data bank.
RN   [4] {ECO:0007829|PDB:4WRR}
RP   X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RA   Hou J., Zheng H., Cooper D.R., Zimmerman M.D., Minor W.;
RT   "Crystal structure of a putative diacylglycerol kinase from Bacillus
RT   anthracis str. Sterne.";
RL   Submitted (OCT-2014) to the PDB data bank.
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; AE017334; AAT34198.1; -; Genomic_DNA.
DR   RefSeq; WP_000167888.1; NZ_WXXJ01000027.1.
DR   PDB; 3S40; X-ray; 2.10 A; A/B/C/D=1-300.
DR   PDB; 3T5P; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-300.
DR   PDB; 4WRR; X-ray; 2.16 A; A/B/C/D=1-300.
DR   AlphaFoldDB; A0A6L8P1L2; -.
DR   SMR; A0A6L8P1L2; -.
DR   IntAct; A0A6L8P1L2; 1.
DR   GeneID; 45024683; -.
DR   KEGG; bar:GBAA_5075; -.
DR   PATRIC; fig|1392.230.peg.5001; -.
DR   OMA; MNGQYIG; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000000594; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3S40, ECO:0007829|PDB:3T5P};
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, ECO:0007829|PDB:3T5P};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..135
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3T5P, ECO:0007829|PDB:4WRR"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3T5P, ECO:0007829|PDB:4WRR"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3T5P, ECO:0007829|PDB:4WRR"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3T5P"
SQ   SEQUENCE   300 AA;  32853 MW;  63CBE1FD016F4140 CRC64;
     MTKTKFEKVL LIVNPKAGQG DLHTNLTKIV PPLAAAFPDL HILHTKEQGD ATKYCQEFAS
     KVDLIIVFGG DGTVFECTNG LAPLEIRPTL AIIPGGTCND FSRTLGVPQN IAEAAKLITK
     EHVKPVDVAK ANGQHFLNFW GIGLVSEVSN NIDAEEKAKL GKIGYYLSTI RTVKNAETFP
     VKITYDGQVY EDEAVLVMVG NGEYLGGIPS FIPNVKCDDG TLDIFVVKST GIQAFKDYIG
     KKLFEDSNEN DIFHVKAKSI HIETEEEKEV DTDGESSLHT PCQIELLQGH FTMIYNPAVV
//