P03004 · DNAA_ECOLI
- ProteinChromosomal replication initiator protein DnaA
- GenednaA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids467 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA-ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring only 1 round of replication per cell cycle. DnaA can inhibit its own gene expression as well as that of other genes such as dam, rpoH, ftsA and mioC.
Also required for replication of plasmid DNA; binds 4 dnaA boxes in the minimal plasmid RK2 replication origin (oriV).
Miscellaneous
At least 4 systems specifically target DnaA to prevent more than 1 round of replication initiation per cell cycle. 1: SeqA binds to and sequesters hemimethylated oriC, preventing DnaA binding. 2: ATP-DnaA binds to the chromosomal datA locus, sequestering ATP-DnaA. 3: ATP-DnaA binds to its own promoter, repressing transcription. 4: RIDA (regulatory inactivation of DnaA) via Hda and the DNA-loaded beta clamp hydrolyzes ATP-DnaA to ADP-DnaA.
Activity regulation
Acetylation decreases the binding abilities to ATP and ADP and leads to inhibition of DNA replication initiation.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | cytosol | |
Cellular Component | DnaA-DiaA complex | |
Cellular Component | DnaA-Dps complex | |
Cellular Component | DnaA-HU complex | |
Cellular Component | DnaA-L2 complex | |
Cellular Component | DnaA-oriC complex | |
Cellular Component | plasma membrane | |
Cellular Component | replication inhibiting complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA replication origin binding | |
Molecular Function | identical protein binding | |
Molecular Function | sequence-specific DNA binding | |
Biological Process | DNA replication | |
Biological Process | DNA replication initiation | |
Biological Process | DNA unwinding involved in DNA replication | |
Biological Process | negative regulation of DNA-templated DNA replication initiation | |
Biological Process | positive regulation of DNA-templated DNA replication initiation | |
Biological Process | regulation of DNA replication | |
Biological Process | regulation of DNA-templated DNA replication initiation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromosomal replication initiator protein DnaA
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP03004
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 178 | Loses the ability to bind to ATP or ADP. | ||||
Sequence: K → Q or R |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000114174 | 1-467 | Chromosomal replication initiator protein DnaA | |||
Sequence: MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSDNTLALYAPNRFVLDWVRDKYLNNINGLLTSFCGADAPQLRFEVGTKPVTQTPQAAVTSNVAAPAQVAQTQPQRAAPSTRSGWDNVPAPAEPTYRSNVNVKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNGIMARKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENDIRLPGEVAFFIAKRLRSNVRELEGALNRVIANANFTGRAITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQMAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDFSNLIRTLSS | ||||||
Modified residue | 178 | N6-acetyllysine; by PatZ | ||||
Sequence: K |
Post-translational modification
Acetylated at Lys-178 by PatZ. Deacetylated by CobB. Is also acetylated nonenzymatically by acetyl-phosphate. Acetylation level increases in a growth phase-dependent manner and peaks at the stationnary phase.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Some 20 DnaA protein molecules bind their sites in oriC. Forms the RIDA (regulatory inactivation of DnaA) complex with ATP-DnaA, ADP-Hda and the DNA-loaded sliding beta clamp (dnaN). Interacts with DiaA; this stimulates the association of DnaA with the origin of replication.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P03004 | diaA P66817 | 5 | EBI-548951, EBI-1125806 | |
BINARY | P03004 | dnaA P03004 | 2 | EBI-548951, EBI-548951 | |
BINARY | P03004 | dnaB P0ACB0 | 4 | EBI-548951, EBI-548978 | |
BINARY | P03004 | dps P0ABT2 | 2 | EBI-548951, EBI-549640 | |
BINARY | P03004 | hda P69931 | 2 | EBI-548951, EBI-545453 | |
BINARY | P03004 | hupA P0ACF0 | 5 | EBI-548951, EBI-547648 | |
BINARY | P03004 | nadE P18843 | 3 | EBI-548951, EBI-548960 | |
BINARY | P03004 | rplB P60422 | 5 | EBI-548951, EBI-543515 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 98-114 | Polar residues | ||||
Sequence: PAQVAQTQPQRAAPSTR | ||||||
Region | 98-119 | Disordered | ||||
Sequence: PAQVAQTQPQRAAPSTRSGWDN |
Sequence similarities
Belongs to the DnaA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length467
- Mass (Da)52,551
- Last updated1993-07-01 v2
- Checksum607C8366A8CDCCED
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 69-70 | in Ref. 1 | ||||
Sequence: AD → RI | ||||||
Compositional bias | 98-114 | Polar residues | ||||
Sequence: PAQVAQTQPQRAAPSTR | ||||||
Sequence conflict | 403-407 | in Ref. 3; AAA62053 | ||||
Sequence: VARPR → GXGPG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01602 EMBL· GenBank· DDBJ | AAB59149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X01861 EMBL· GenBank· DDBJ | CAA25980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L10328 EMBL· GenBank· DDBJ | AAA62053.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC76725.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77592.1 EMBL· GenBank· DDBJ | Genomic DNA |