DnaB is the hexameric ATP-dependent replicative DNA helicase. It translocates 5'-to-3' on one DNA strand ahead of the bacterial replisome, coupling ATP hydrolysis to parental-duplex unwinding during chromosome-replication initiation and elongation. DnaB also recruits and stimulates DnaG primase during primer synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000104 | MARK AS OVER ANNOTATED | Summary: True but nonspecific relative to ATP binding and ATP-dependent helicase activity. Reason: DnaB is specifically an ATP-dependent P-loop helicase, so generic nucleotide binding adds little value. |
| GO:0003677 DNA binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Correct substrate interaction for a replicative DNA helicase. Reason: DnaB binds and translocates on DNA while unwinding the parental duplex. |
| GO:0003678 DNA helicase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core molecular function. Reason: The local UniProt record identifies DnaB as the main ATP-dependent replicative DNA helicase. |
| GO:0004386 helicase activity | IEA GO_REF:0000104 | MARK AS OVER ANNOTATED | Summary: Correct but broader than the DNA-specific helicase terms. Reason: GO:0003678 and GO:0043139 capture the relevant substrate and directionality. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: Correct nucleotide-binding property required for helicase action. Reason: DnaB is an ATP-dependent P-loop helicase. |
| GO:0005829 cytosol | IEA GO_REF:0000118 | ACCEPT | Summary: Appropriate localization for the bacterial replicative helicase. Reason: DnaB operates at chromosome-replication forks in the cytosol/nucleoid. |
| GO:0006260 DNA replication | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core biological process. Reason: DnaB unwinds parental DNA during both initiation and elongation of chromosome replication. |
| GO:0006269 DNA replication, synthesis of primer | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: The target record places DnaB in the primosome and assigns primer synthesis, but helicase activity remains its defining role. Reason: The biological-process annotation does not assert that DnaB catalyzes RNA synthesis. The target UniProt record assigns both primosome-complex membership and this primer-synthesis process, supporting retention as non-core without inferring an undocumented target-specific interaction. Supporting Evidence: file:PSEPK/dnaB/dnaB-uniprot.txt GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule. |
| GO:0016787 hydrolase activity | IEA GO_REF:0000104 | MARK AS OVER ANNOTATED | Summary: True but uninformative parent activity. Reason: ATP hydrolysis and directional DNA helicase activity provide the relevant mechanistic specificity. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct ATPase activity coupled to DNA unwinding. Reason: The local UniProt record explicitly describes DNA-dependent ATP hydrolysis by DnaB. |
| GO:0043139 5'-3' DNA helicase activity | IEA GO_REF:0000003 | ACCEPT | Summary: Correct specific core activity and translocation polarity. Reason: DnaB is a processive 5'-to-3' DNA helicase at the bacterial replication fork. |
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Download this section (compressed HTML)Consulted the annotation-reviewer workflow against all 11 current GOA rows, UniProt Q88DF2, EC 5.6.2.3, and the DnaB domain assignments. Accepted DNA helicase activity, ATP binding/hydrolysis, cytosolic localization, DNA replication, and the specific 5'-3' helicase activity; retained generic DNA binding as non-core. Marked generic nucleotide binding, helicase activity, and hydrolase activity as over-annotated. Primer synthesis is retained as non-core because the target record assigns that process and primosome-complex membership, without using those automated assignments to infer a target-specific interaction mechanism. No GOA row remains pending.
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