Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.101 - DNA primase DnaG and Organism(s) Bacillus subtilis and UniProt Accession P05096

for references in articles please use BRENDA:EC2.7.7.101
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.101 DNA primase DnaG
IUBMB Comments
The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: P05096
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
+
n
=
ssDNA/pppN(pN)n-1 hybrid
+
(n-1)
Synonyms
primase dnag, ssodnag, dna primase dnag, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DnaG primase-A
-
DnaG
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleotide 5'-triphosphate:single-stranded DNA nucleotidyltransferase (DNA-RNA hybrid synthesizing)
The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-(6-chloro-2H-chromen-3-yl)acrylic acid
-
-
2-((1H-indol-3-yl)thio)acetic acid
-
-
2-fluoro-AraATP
-
-
3-[2-(ethoxycarbonyl)-5-nitro-1H-indol-3-yl]propanoic acid
-
-
4-fluorophenyl tetrazole
-
-
7-nitro-1H-indole-2-carboxylic acid
-
BAY 57-1293
-
-
benzo[d]imidazo[2,1-b]imidazole
lead structure for inhibitor search
-
benzo[d]pyrimido[5,4-b]furan
lead structure for inhibitor search
-
cytosporone D
-
-
pyrido[3',2'4,5]thieno[3,2-d]pyrimidine
lead structure for inhibitor search
-
additional information
inhibitor screening
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
sequence and structural homology of DnaG-like primases, overview
malfunction
inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
physiological function
physiological function
-
DnaG physically interacts with bacteriophage SPP1 hexameric helicase G40P (G40P6) in the absence of ATP. The presence of DnaG in the reaction mixture increases the helicase activity of G40P6 about 3fold, but not the ATPase activity
additional information
structure function relationship of DnaG primase, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 68800, calculated from sequence, 1 * 69000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the RNA polymerase domain of DnaG. The tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. The ssDNA template binding surface is L-shaped, a model for the template ssDNA binding to primase is proposed. Comparison with the enzyme from Geobacillus stearothermophilus
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K232A
more than 50% decrease in DNA binding activity
N235A
loss of DNA binding activity
R148A
mutation slightly affects DNA binding activity
R202A
mutation significantly affects DNA binding activity
R204A
mutation significantly affects DNA binding activity
R224A
more than 50% decrease in DNA binding activity
W167A
mutation significantly affects DNA binding activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduced recombinant polypeptide is insoluble, aggregates can be dissolved in the presence of 3 M urea
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ayora, S.; Langer, U.; Alonso, J.
Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex
FEBS Lett.
439
59-62
1998
Bacillus subtilis
-
Manually annotated by BRENDA team
Rannou, O.; Le Chatelier, E.; Larson, M.A.; Nouri, H.; Dalmais, B.; Laughton, C.; Janniere, L.; Soultanas, P.
Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis
Nucleic Acids Res.
41
5303-5320
2013
Bacillus subtilis (P05096), Bacillus subtilis, Bacillus subtilis 168 (P05096)
Manually annotated by BRENDA team
Zhou, Y.; Luo, H.; Liu, Z.; Yang, M.; Pang, X.; Sun, F.; Wang, G.
Structural insight into the specific DNA template binding to DnaG primase in bacteria
Sci. Rep.
7
659
2017
Bacillus subtilis (P05096), Bacillus subtilis 168 (P05096)
Manually annotated by BRENDA team
Ilic, S.; Cohen, S.; Singh, M.; Tam, B.; Dayan, A.; Akabayov, B.
DnaG primase-A target for the development of novel antibacterial agents
Antibiotics
7
72
2018
Bacillus subtilis (P05096), Bacillus subtilis 168 (P05096), Escherichia coli (P0ABS5), Mycobacterium tuberculosis (P9WNW1), Mycobacterium tuberculosis ATCC 25618 (P9WNW1), Mycobacterium tuberculosis H37Rv (P9WNW1)
Manually annotated by BRENDA team