ID   YTLR_BACSU              Reviewed;         309 AA.
AC   O34799; Q795S5;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Putative lipid kinase YtlR;
DE            EC=2.7.1.-;
GN   Name=ytlR; OrderedLocusNames=BSU29940;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   LACK OF FUNCTION AS A DIACYLGLYCEROL KINASE.
RX   PubMed=17535816; DOI=10.1074/jbc.m703536200;
RA   Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT   "Identification of a soluble diacylglycerol kinase required for
RT   lipoteichoic acid production in Bacillus subtilis.";
RL   J. Biol. Chem. 282:21738-21745(2007).
CC   -!- FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids
CC       other than diacylglycerol (DAG). In fact, is not able to exhibit
CC       diacylglycerol kinase activity in vitro.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC       structural role and is required for catalytic activity. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF008220; AAC00282.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14972.1; -; Genomic_DNA.
DR   PIR; H69995; H69995.
DR   RefSeq; NP_390872.1; NC_000964.3.
DR   RefSeq; WP_003229243.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34799; -.
DR   SMR; O34799; -.
DR   STRING; 224308.BSU29940; -.
DR   PaxDb; O34799; -.
DR   PRIDE; O34799; -.
DR   EnsemblBacteria; CAB14972; CAB14972; BSU_29940.
DR   GeneID; 937289; -.
DR   KEGG; bsu:BSU29940; -.
DR   PATRIC; fig|224308.179.peg.3252; -.
DR   eggNOG; COG1597; Bacteria.
DR   InParanoid; O34799; -.
DR   OMA; NDFAKYW; -.
DR   PhylomeDB; O34799; -.
DR   BioCyc; BSUB:BSU29940-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10330; -; 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   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   TIGRFAMs; TIGR00147; TIGR00147; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..309
FT                   /note="Putative lipid kinase YtlR"
FT                   /id="PRO_0000386483"
FT   DOMAIN          1..134
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         9..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         69..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  35608 MW;  34C9B7FBD367E40E CRC64;
     MSHWFFIINP TAGHRNGLRV WKSIQKELIK RKVEHRSFLT EHPGHAEVLA RQISTIQEYK
     LKRLIVIGGD GTMHEVVNGL KDVDDIELSF VPAGAYNDFS RGFSIKKIDL IQEIKKVKRP
     LTRTFHLGSV NFLQDKSQIL YFMNHIGIGF DAYVNKKAME FPLRRVFLFL RLRFLVYPLS
     HLHASATFKP FTLACTTEDE TREFHDVWFA VVSNHPFYGG GMKAAPLANP REKTFDIVIV
     ENQPFLKKYW LLCLMAFGKH TKMDGVTMFK AKDITFYTKD KIPFHADGEI MGTTPFRLAS
     SPSPLRIKT