UDPK_BACSU
ID UDPK_BACSU Reviewed; 123 AA.
AC P19638;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Undecaprenol kinase;
DE Short=UdpK;
DE EC=2.7.1.66;
GN Name=dgkA; Synonyms=dgk, yqxF; OrderedLocusNames=BSU25310;
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=ED40;
RA Kim K., Hwang S., Suh J., Song B.-H., Hong S., Kim J.;
RT "Nucleotide sequence upstream of the cdd locus in Bacillus subtilis.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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 N-TERMINUS.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123.
RC STRAIN=168;
RX PubMed=2526291; DOI=10.1007/bf00334391;
RA Song B.-H., Neuhard J.;
RT "Chromosomal location, cloning and nucleotide sequence of the Bacillus
RT subtilis cdd gene encoding cytidine/deoxycytidine deaminase.";
RL Mol. Gen. Genet. 216:462-468(1989).
RN [6]
RP IDENTIFICATION.
RX PubMed=8071224; DOI=10.1128/jb.176.17.5459-5465.1994;
RA Smith R.L., O'Toole J.F., Maguire M.E., Sanders C.R. II;
RT "Membrane topology of Escherichia coli diacylglycerol kinase.";
RL J. Bacteriol. 176:5459-5465(1994).
RN [7]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12923107; DOI=10.1128/jb.185.17.5306-5309.2003;
RA Amiteye S., Kobayashi K., Imamura D., Hosoya S., Ogasawara N., Sato T.;
RT "Bacillus subtilis diacylglycerol kinase (DgkA) enhances efficient
RT sporulation.";
RL J. Bacteriol. 185:5306-5309(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15743965; DOI=10.1128/jb.187.6.2163-2174.2005;
RA Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
RT "Phosphatidylethanolamine domains and localization of phospholipid
RT synthases in Bacillus subtilis membranes.";
RL J. Bacteriol. 187:2163-2174(2005).
RN [9]
RP FUNCTION AS AN UNDECAPRENOL KINASE, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
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: Catalyzes the phosphorylation of undecaprenol in vitro, which
CC is probably the physiological substrate. Exhibits no detectable
CC activity against other substrates such as monoacylglycerol, ceramide,
CC or diacylglycerol (DAG). Appears indispensable for the maintenance of
CC spore stability and viability in B.subtilis.
CC {ECO:0000269|PubMed:17535816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + di-trans,octa-cis-undecaprenol = ADP + di-trans,octa-
CC cis-undecaprenyl phosphate + H(+); Xref=Rhea:RHEA:28122,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:61216, ChEBI:CHEBI:456216; EC=2.7.1.66;
CC Evidence={ECO:0000269|PubMed:17535816};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Localized in both lateral and septal
CC membranes. {ECO:0000269|PubMed:15743965}.
CC -!- INDUCTION: Mainly expressed during the vegetative phase of growth.
CC {ECO:0000269|PubMed:12923107}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit an abnormal
CC cortex structure in mutant endospores 6 hours after the onset of
CC sporulation, an indication of cortex degeneration. In addition, they
CC display a significant decrease in the dipicolinic acid content of
CC mutant spores. {ECO:0000269|PubMed:12923107}.
CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a diacylglycerol kinase.
CC {ECO:0000305|PubMed:12923107}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70044.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA12480.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U29177; AAA70044.1; ALT_INIT; Genomic_DNA.
DR EMBL; D84432; BAA12480.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB14460.2; -; Genomic_DNA.
DR EMBL; X17430; CAB57857.1; -; Genomic_DNA.
DR PIR; G69614; G69614.
DR RefSeq; NP_390409.2; NC_000964.3.
DR RefSeq; WP_004398824.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P19638; -.
DR SMR; P19638; -.
DR STRING; 224308.BSU25310; -.
DR SwissLipids; SLP:000001807; -.
DR PaxDb; P19638; -.
DR PRIDE; P19638; -.
DR EnsemblBacteria; CAB14460; CAB14460; BSU_25310.
DR GeneID; 937873; -.
DR KEGG; bsu:BSU25310; -.
DR PATRIC; fig|224308.179.peg.2751; -.
DR eggNOG; COG0818; Bacteria.
DR InParanoid; P19638; -.
DR OMA; SFRYAAQ; -.
DR PhylomeDB; P19638; -.
DR BioCyc; BSUB:BSU25310-MON; -.
DR BioCyc; MetaCyc:BSU25310-MON; -.
DR BRENDA; 2.7.1.107; 658.
DR BRENDA; 2.7.1.66; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036433; F:di-trans, poly-cis-undecaprenol kinase activity; IEA:RHEA.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd14265; UDPK_IM_like; 1.
DR Gene3D; 1.10.287.3610; -; 1.
DR InterPro; IPR000829; DAGK.
DR InterPro; IPR036945; DAGK_sf.
DR InterPro; IPR033717; UDPK.
DR PANTHER; PTHR34299; PTHR34299; 1.
DR Pfam; PF01219; DAGK_prokar; 1.
DR PROSITE; PS01069; DAGK_PROKAR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Sporulation; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..123
FT /note="Undecaprenol kinase"
FT /id="PRO_0000195259"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 112
FT /note="C -> S (in Ref. 1; AAA70044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 13639 MW; 7BED3954910AEBF9 CRC64;
MDSKDHRNEL NRFFKSFVHA GRGIWETART ERNFQFHAAA ACAVLICGFL VELSIIEWMI
IFLLIGGMFS LELLNTAIEH TVDLITDKHH PLAKAAKDAA AGAVCVFAVI SCIIGLLIFL
PKL
