{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P03004","secondaryAccessions":["P78122","Q2M814"],"uniProtkbId":"DNAA_ECOLI","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-07-01","entryVersion":211,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"value":"Chromosomal replication initiator protein DnaA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15878847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3036372"}],"value":"3.6.4.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"value":"dnaA"},"orderedLocusNames":[{"value":"b3702"},{"value":"JW3679"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O66659"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2540187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26272946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2981626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3036372"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9478970"}],"value":"Plays an essential 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 once per cell cycle (PubMed:3036372). Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3') and separates the double-stranded (ds)DNA (PubMed:3036372, PubMed:18216012). Forms a right-handed helical filament on oriC DNA; dsDNA binds to the exterior of the filament while single-stranded (ss)DNA is stabiized in the filament's interior (By similarity). The ATP-DnaA-oriC complex binds and stabilizes the upper strand of the AT-rich DNA unwinding element (DUE) (PubMed:18216012). Mutagenesis of residues that line the central pore blocks dsDNA strand separation (PubMed:18216012). Subsequent binding of DNA polymerase III subunits leads to replisome formation (PubMed:3036372, PubMed:18216012). 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 (PubMed:3036372). Binds ATP, ADP and dATP equally well, hydrolyzes ATP with a half-life of about 15 minutes, ATP hydrolysis is not required for pre-priming replisome formation, nucleotide exchange is very slow (PubMed:3036372). Binds acidic phospholipids (PubMed:9478970, PubMed:26272946). DnaA inhibits its own gene expression (PubMed:2981626) as well as that of other genes including dam, rpoH (PubMed:2540187), ftsA and mioC"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15878847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9242693"}],"value":"Also required for replication of some plasmid DNA; binds 4 DnaA boxes in the minimal plasmid RK2 replication origin (oriV)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15878847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3036372"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18977760"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19401329"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27484197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9674428"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26272946"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9478970"}],"value":"Inactivated in part by the RIDA complex (regulatory inactivation of DnaA), composed of ATP-DnaA, Hda and the DNA-loaded beta sliding clamp (dnaN), which rapidly hydrolyzes ATP-DnaA to ADP-DnaA in a DNA-dependent fashion, preventing reinitiation of DNA replication (PubMed:9674428, PubMed:18977760). DnaA inactivation by RIDA is further stimulated by DNA synthesis (PubMed:9674428). Also inactivated by IHF in combination with the datA locus, which promotes ATP hydrolysis of ATP-DnaA, called DDAH (datA-dependent DnaA-ATP hydrolysis) (PubMed:23277577). Reactivation/rejuvenation of ATP-DnaA occurs by binding to specific chromosomal loci called DARS (DnaA reactivating sequences), which promote ADP release from ADP-DnaA (PubMed:19401329). DARS1 and DARS2 act independently to elevate the ATP-DnaA level in vivo; their deletion inhibits replication initiation (PubMed:19401329). Rejuvenation of ATP-DnaA may also occur in part on the cell inner membrane (PubMed:9478970, PubMed:26272946). Acetylation decreases the binding abilities to ATP and ADP and leads to inhibition of DNA replication initiation (PubMed:27484197)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17699754"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18977760"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9674428"}],"value":"Oligomerizes as a right-handed, spiral filament on DNA at oriC (By similarity). About 20 DnaA protein molecules bind to oriC. Forms the RIDA (regulatory inactivation of DnaA) complex with ATP-DnaA, ADP-Hda and the DNA-loaded sliding beta clamp (dnaN) (PubMed:9674428, PubMed:18977760). Interacts with DiaA; this stimulates the association of DnaA with the origin of replication (PubMed:17699754)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P66817","geneName":"diaA","intActId":"EBI-1125806"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P03004","geneName":"dnaA","intActId":"EBI-548951"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P0ACB0","geneName":"dnaB","intActId":"EBI-548978"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P0ABT2","geneName":"dps","intActId":"EBI-549640"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P69931","geneName":"hda","intActId":"EBI-545453"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P0ACF0","geneName":"hupA","intActId":"EBI-547648"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P18843","geneName":"nadE","intActId":"EBI-548960"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P03004","intActId":"EBI-548951"},"interactantTwo":{"uniProtKBAccession":"P60422","geneName":"rplB","intActId":"EBI-543515"},"numberOfExperiments":5,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28166228"}],"value":"About 10% of the protein associates with the cell inner membrane (shown in strain BL21(DE3)) (PubMed:22574163). 70% of the protein oscillates between opposite cell halves in a time frame of a few seconds, independent of transcription (PubMed:28166228)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28166228"}],"value":"Cytoplasm, nucleoid","id":"SL-0187"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9478970"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2981626"}],"value":"Part of the dnaA-dnaN-recF-gyrB operon. Represses its own transcription; has 2 promoters, both of which are autorepressed (PubMed:2981626). DnaA binds within its own promoter (PubMed:2981626)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12682358"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15878847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9478970"}],"value":"Domain I is involved in oligomerization and binding regulators, domain II is flexibile and of varying length in different bacteria, domain III forms the AAA+ region, while domain IV binds dsDNA (PubMed:15878847). Binds to the inner membrane via domain III (residues 117-378) (PubMed:22574163). Binds dsDNA via domain IV (PubMed:12682358). Inserts into acidic phosopholipid-containing membranes via resides 309-399 which plays a role in rejuventation of ATP-DnaA (PubMed:9478970)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27484197"}],"value":"Acetylated at Lys-178 by PatZ (PubMed:27484197). Deacetylated by CobB (PubMed:27484197). Is also acetylated nonenzymatically by acetyl-phosphate (PubMed:27484197). Acetylation levels increase in a growth phase-dependent manner and peak in stationary phase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18977760"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2981626"}],"value":"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, hydrolyzing ATP-DnaA in the presence of IHF (PubMed:23277577). 3: ATP-DnaA binds to its own promoter, repressing transcription (PubMed:2981626). 4: RIDA (regulatory inactivation of DnaA) via Hda and the DNA-loaded beta clamp (dnaN) hydrolyzes ATP-DnaA to ADP-DnaA (PubMed:18977760)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"value":"Belongs to the DnaA family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAA62053.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Chromosomal replication initiator protein DnaA","featureId":"PRO_0000114174"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Domain I, interacts with DnaA modulators","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15878847"}]},{"type":"Region","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Domain II, transiently binds replication helicase","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15878847"}]},{"type":"Region","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"Domain III, AAA+ region","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15878847"}]},{"type":"Region","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Inserts into membranes","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9478970"}]},{"type":"Region","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Domain IV, binds dsDNA","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12682358"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15878847"}]},{"type":"Compositional bias","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00377"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"N6-acetyllysine; by PatZ","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27484197"}]},{"type":"Mutagenesis","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"Unable to initiate replication from oriC or oriV, no self-oligomerization, binds DNA normally, no change in ATPase or ATP affinity, cannot load DnaB helicase.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15878847"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Inactive for DNA replication in vivo, wild-type affinity for ADP and ATP, does not load DnaB helicase.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17420252"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"In dnaA167; temperature sensitive.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6234204"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Loses the ability to bind to ATP or ADP.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27484197"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["Q","R"]}},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"In dnaA46; temperature sensitive.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6234204"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["V"]}},{"type":"Mutagenesis","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Does not initiate replication at oriC at 42 degrees Celsius, does not unwind oriC, forms active ATP-DnaA-oriC complex, does not bind ssDNA, can load DnaB helicase, ATP- and DNA-binding are wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216012"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Does not initiate replication at oriC at 42 degrees Celsius, does not unwind oriC, does not form active ATP-DnaA-oriC complex, can load DnaB helicase, ATP- and DNA-binding are wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216012"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"Does not initiate replication at oriC at 30 degrees Celsius, does not unwind oriC, does not form active ATP-DnaA-oriC complex, poor loading of DnaB helicase, ATP- and DNA-binding are wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216012"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Does not initiate replication at oriC at 30 degrees Celsius, does not unwind oriC, forms active ATP-DnaA-oriC complex, does not bind ssDNA, can load DnaB helicase, ATP- and DNA-binding are wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216012"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"DARS1 no longer stimulates ADP release from ADP-DnaA, binds DNA but forms fewer complexes with DARS1 DNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19401329"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"ATP-DnaA poorly hydrolyzed by datA-IHF.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Moderate decrease in DARS1-mediated ADP release from ADP-DnaA, binds DARS1 DNA normally. ATP-DnaA poorly hydrolyzed by datA-IHF.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19401329"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"ATP-DnaA is no longer hydrolyzed by datA-IHF.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"DARS1 no longer stimulates ADP release from ADP-DnaA, does not bind DNA. ATP-DnaA is no longer hydrolyzed by datA-IHF.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19401329"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23277577"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Decreased DNA-binding; protein does not localize to the nucleoid, forms inclusion bodies at cell pole(s).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22574163"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["P"]}},{"type":"Mutagenesis","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"DARS1 no longer stimulates ADP release from ADP-DnaA, does not bind 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