(data stored in SCRATCH zone)

SWISSPROT: BMRU_BACSU

ID   BMRU_BACSU              Reviewed;         297 AA.
AC   P39074;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=Putative lipid kinase BmrU;
DE            EC=2.7.1.-;
GN   Name=bmrU; OrderedLocusNames=BSU24000;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=7961792;
RA   Ahmed M., Borsch C.M., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.;
RT   "A protein that activates expression of a multidrug efflux transporter upon
RT   binding the transporter substrates.";
RL   J. Biol. Chem. 269:28506-28513(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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   [4]
RP   SEQUENCE REVISION TO 15; 47 AND 95.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
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}.
DR   EMBL; L25604; AAB81538.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12602.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14331.2; -; Genomic_DNA.
DR   PIR; F69595; F69595.
DR   RefSeq; NP_390280.2; NC_000964.3.
DR   RefSeq; WP_003230330.1; NZ_JNCM01000036.1.
DR   SMR; P39074; -.
DR   STRING; 224308.BSU24000; -.
DR   PaxDb; P39074; -.
DR   PRIDE; P39074; -.
DR   EnsemblBacteria; CAB14331; CAB14331; BSU24000.
DR   GeneID; 938679; -.
DR   KEGG; bsu:BSU24000; -.
DR   PATRIC; fig|224308.179.peg.2614; -.
DR   eggNOG; ENOG4109050; Bacteria.
DR   eggNOG; COG1597; LUCA.
DR   HOGENOM; HOG000261395; -.
DR   InParanoid; P39074; -.
DR   OMA; LPGGTCN; -.
DR   PhylomeDB; P39074; -.
DR   BioCyc; BSUB:BSU24000-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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   Pfam; PF00781; DAGK_cat; 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;
DR   PRODOM; P39074.
DR   SWISS-2DPAGE; P39074.
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..297
FT                   /note="Putative lipid kinase BmrU"
FT                   /id="PRO_0000064954"
FT   DOMAIN          1..132
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   NP_BIND         67..73
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   METAL           213
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           216
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           218
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         94
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   CONFLICT        15
FT                   /note="G -> A (in Ref. 1; AAB81538 and 2; BAA12602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="D -> H (in Ref. 1; AAB81538 and 2; BAA12602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="C -> S (in Ref. 1; AAB81538 and 2; BAA12602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  32441 MW;  78760594947DB6F4 CRC64;
     MSHRKALLIH NGNAGNKNIE KALGAVVPVL SHHLDEVIIK QTKKKDDAYH FCRSIDDSVD
     TVFILGGDGT IHQCINAISA LERKPAVGIL PGGTCNDFSR VLGIPQNLAK AAEALMAGKK
     TSVDVCQMND RYFLNFWGIG LIAETSNQIN ETEKALLGKI SYFTSALRTV SSAASFPMTL
     KIDGEEIKEE AVMLLVMNGQ YIGTNRIPLP DASIEDGLLD VLICRNTNLT ALRELMSMEQ
     GSIDRFTGEL SYVQASRIEI ETDTAKKADM DGEVYTHTPA VIQVLPQHID MLVPANE
//

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