UDPK_STRMU
ID UDPK_STRMU Reviewed; 137 AA.
AC Q05888; O51807;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Undecaprenol kinase;
DE Short=UdpK;
DE EC=2.7.1.66;
GN Name=dgkA; Synonyms=dgk; OrderedLocusNames=SMU_1618;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=GS-5;
RX PubMed=8407794; DOI=10.1128/jb.175.19.6220-6228.1993;
RA Yamashita Y., Takehara T., Kuramitsu H.K.;
RT "Molecular characterization of a Streptococcus mutans mutant altered in
RT environmental stress responses.";
RL J. Bacteriol. 175:6220-6228(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=T8;
RX PubMed=9422608; DOI=10.1128/jb.180.1.167-170.1998;
RA Chen P., Novak J., Qi F.-Q., Caufield P.W.;
RT "Diacylglycerol kinase is involved in regulation of expression of the
RT lantibiotic mutacin II of Streptococcus mutans.";
RL J. Bacteriol. 180:167-170(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=GS-5;
RX PubMed=12654811; DOI=10.1128/iai.71.4.1938-1943.2003;
RA Lis M., Kuramitsu H.K.;
RT "The stress-responsive dgk gene from Streptococcus mutans encodes a
RT putative undecaprenol kinase activity.";
RL Infect. Immun. 71:1938-1943(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of undecaprenol, which is
CC probably the primary physiological substrate. Is also able to
CC phosphorylate diacylglycerol, albeit with very low efficiency. May play
CC a role in adaptability to environmental stress conditions such as acid
CC tolerance, elevated temperatures and high osmolarity.
CC {ECO:0000269|PubMed:12654811}.
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:12654811};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12654811};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12654811}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display defective growth
CC at low pH, elevated temperatures, and high osmolarity. Moreover, they
CC exhibit a significant reduction in the transcription level of mutA and
CC a defect in production of the lantibiotic mutacin II. They also show
CC reduced resistance to bacitracin. {ECO:0000269|PubMed:12654811,
CC ECO:0000269|PubMed:8407794, ECO:0000269|PubMed:9422608}.
CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L12211; AAA26867.1; -; Genomic_DNA.
DR EMBL; AF000954; AAC38047.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59259.1; -; Genomic_DNA.
DR PIR; A36933; A36933.
DR RefSeq; NP_721953.1; NC_004350.2.
DR AlphaFoldDB; Q05888; -.
DR SMR; Q05888; -.
DR STRING; 210007.SMU_1618; -.
DR EnsemblBacteria; AAN59259; AAN59259; SMU_1618.
DR KEGG; smu:SMU_1618; -.
DR PATRIC; fig|210007.7.peg.1441; -.
DR eggNOG; COG0818; Bacteria.
DR HOGENOM; CLU_112343_2_2_9; -.
DR OMA; SFRYAAQ; -.
DR PhylomeDB; Q05888; -.
DR BRENDA; 2.7.1.66; 5941.
DR Proteomes; UP000002512; 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 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; Stress response; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..137
FT /note="Undecaprenol kinase"
FT /id="PRO_0000195269"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 128..129
FT /note="VP -> LL (in Ref. 1; AAA26867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15350 MW; 5471974885319125 CRC64;
MPMDLRDNKQ SQKKWKNRTL TSSLEFALTG IFTAFKEERN MKKHAVSALL AVIAGLVFKV
SVIEWLFLLL SIFLVITFEI VNSAIENVVD LASDYHFSML AKNAKDMAAG AVLVISGFAA
LTGLIIFVPK IWFLLFH
