{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P07908","uniProtkbId":"DNAB_BACSU","entryAudit":{"firstPublicDate":"1988-08-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1988-08-01","entryVersion":146,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Bacillus subtilis (strain 168)","taxonId":224308,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32817095"}],"value":"Replicative helicase loading/DNA remodeling protein DnaB"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3027697"}],"value":"Replication initiation and membrane attachment protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12718886"}],"value":"Replicative helicase loader DnaB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3027671"}],"value":"dnaB"},"orderedLocusNames":[{"value":"BSU28990"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11679082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12718886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15186423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16002087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19968790"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027671"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027697"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36416272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6771760"}],"value":"Helps DnaI load the DnaC replicative helicase onto single-stranded (ss)DNA (PubMed:12718886). During DNA replication from the origin of replication (oriC) in the DNA replisome, DnaD is required after DnaA, before DnaB and before subsequent helicase DnaC loading (PubMed:15186423, PubMed:19968790). Component of the replication restart primosome, which reloads the replicative helicase on sites other than oriC (PubMed:11585815). DnaB, DnaD and DnaI may also be required for a PriA-independent pathway of replication fork restart (PubMed:11679082). DnaB and DnaD work together to allow DnaB access to ssDNA (PubMed:15686560). DNA replication at oriC might originate on the inner face of the cell membrane; DnaB is essential for both replication initiation and cell membrane attachment of the origin region of the chromosome and plasmids (PubMed:6771760, PubMed:3027671, PubMed:3027697). Weakly binds ssDNA (PubMed:11585815, PubMed:15686560, PubMed:32817095), preferentially binds double-stranded (ds)DNA (PubMed:32817095), and replication fork-like substrates (PubMed:11585815). Remodels DNA, laterally compacts supercoiled plasmid and linear DNA, forms beads along the dsDNA (PubMed:16002087). Together DnaB and DnaD form bipolar complexes on plasmid DNA (PubMed:16002087). DnaB and DnaD are also required to load helicase on the repN plasmid origin of replication (oriN) (PubMed:36416272)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11585815"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12718886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15686560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16002087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19968790"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35576203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36416272"}],"value":"Homotetramer (PubMed:11585815, PubMed:12718886, PubMed:16002087, PubMed:20071750, PubMed:32817095). Also forms higher-order oligomers, can be induced by some ssDNA (PubMed:16002087, PubMed:32817095). The DNA replisome assembles sequentially on oriC in this order; DnaA, DnaD, DnaB, DnaI-DnaC helicase (PubMed:19968790). In atomic force microscopy forms a square with a small central hole (PubMed:16002087). Part of the replication restart primosome which assembles in this order; PriA, DnaD then DnaB. The preferred DNA substrate mimics an arrested DNA replication fork with unreplicated lagging strand (PubMed:11585815). Interacts with DnaC, but probably not as a tetramer (PubMed:12718886). Interacts with DnaD (PubMed:15186423, PubMed:15686560, PubMed:36416272) but no interaction with PriA was seen (PubMed:15686560). Interacts with cell cycle regulator CcrZ (PubMed:35576203)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10844689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"}],"value":"Forms foci near both cell poles and in the middle of cells (PubMed:10844689). DnaB interacts with oriC downstream of dnaA, truncated DnaB is specifically depleted at oriC and not other sites in the genome (PubMed:20071750)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10844689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15186423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"}],"value":"Cell membrane","id":"SL-0039"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"}],"value":"Transcribed at constant levels during exponential growth (PubMed:20071750). Present in all growth phases (at protein level) (PubMed:20071750)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20587500"}],"value":"Bind ssDNA via the N-terminus (residues 1-300), which also mediates tetramerization (PubMed:20071750). A region in the C-terminus (residues 365-428) also binds ssDNA, dsDNA and is responsible for DNA-mediated oligomerization (PubMed:20071750). Has 3 domains with homology to DnaD called DDBH1 and DDBH2 (DnaD DnaB Homology 1 and 2) followed by a short positively charged region and a probable C-terminal alpha-helix (PubMed:20587500). Removal of residues 429-472 increases dsDNA and some ssDNA binding, while removal of 312-472 prevents all DNA binding (PubMed:32817095)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20071750"}],"value":"In early growth phase only full-length protein is detected, during late growth and stationary phase full-length and C-terminally truncated proteins are seen (at protein level) (PubMed:20071750). Truncated protein is only seen in cytoplasmic fractions (PubMed:20071750)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19968790"}],"value":"Essential, it cannot be deleted; in depletion experiments DNA replication slows as soon as the protein is degraded and replication stops by 1 hour (PubMed:19968790)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027671"}],"value":"The dna-1 (dnaBI) and dnaB-19 (dnaBII) mutants show different characteristics for replication and membrane binding of plasmid pUB110. DnaBI is essential for both chromosome and pUB110 replication, whereas dnaBII is necessary only for chromosome replication"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20587500"}],"value":"Belongs to the DnaB/DnaD family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Replicative helicase loading/DNA remodeling protein DnaB","featureId":"PRO_0000079950"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"DDBH1","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20587500"}]},{"type":"Region","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"DDBH2-1","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20587500"}]},{"type":"Region","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"DDBH2-2","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20587500"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32817095"}]},{"type":"Region","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Mutagenesis","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"In strain dnaB134; temperature-sensitive for growth. Loss of association of DnaC with oriC at 52 degrees Celsius.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15186423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19968790"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"In dna-1; temperature-sensitive, chromosome inititation is lost, origin region and plasmid no longer associate with cell membrane at 45 degrees Celsius. In dnaBI; required for chromosome and plasmid replication.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027697"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6771760"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"In dnaB27; impairs chromosome replication initiation, the effect is reversible.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027671"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"In dnaB75, also called DnaBS371P; suppresses a deletion of priA, restores plasmid replication, loads DnaC helicase aspecifically, increased affinity for forked DNA. Suppresses dnaB134 and dnaD23 temperature-sensitive mutations, allows detection of DnaB-DnaD interaction, overexpression alters control of replication initiation. Suppresses temperature sensitivity of dnaD23 at 51 degrees Celsius without changing levels of DnaD protein, 50-fold increased ssDNA-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11679082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12718886"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15186423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15686560"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["P"]}},{"type":"Mutagenesis","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"Improved binding of phiX174 ssDNA, increased oligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Improved binding of phiX174 ssDNA, slightly decreased dsDNA binding, greatly increased oligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"}],"alternativeSequence":{"originalSequence":"I","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"In dnaB19; impairs chromosome replication initiation, origin region no longer associates with cell membrane at 45 degrees Celsius. In dnaBII; required only for chromosome replication.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027671"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3027697"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6771760"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["T"]}},{"type":"Mutagenesis","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Improved binding of phiX174 ssDNA, greatly increased oligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817095"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0639","category":"Cellular component","name":"Primosome"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"3027671","citationType":"journal article","authors":["Ogasawara N.","Moriya S.","Mazza P.G.","Yoshikawa H."],"citationCrossReferences":[{"database":"PubMed","id":"3027671"},{"database":"DOI","id":"10.1093/nar/14.24.9989"}],"title":"Nucleotide sequence and organization of dnaB gene and neighbouring genes on the Bacillus subtilis chromosome.","publicationDate":"1986","journal":"Nucleic Acids Res.","firstPage":"9989","lastPage":"9999","volume":"14"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","MUTAGENESIS OF ASP-122 AND ALA-379"],"referenceComments":[{"value":"168","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"3027697","citationType":"journal article","authors":["Hoshino T.","McKenzie T.","Schmidt S.","Tanaka T.","Sueoka N."],"citationCrossReferences":[{"database":"PubMed","id":"3027697"},{"database":"DOI","id":"10.1073/pnas.84.3.653"}],"title":"Nucleotide sequence of Bacillus subtilis dnaB: a gene essential for DNA replication initiation and membrane attachment.","publicationDate":"1987","journal":"Proc. 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