DnaN is the beta sliding clamp of Escherichia coli. A head-to-tail homodimer encircles DNA and tethers DNA polymerases, increasing processivity and coordinating exchanges between replication and repair enzymes. The clamp loader opens and deposits beta on primed DNA. DnaN also recruits Hda in regulatory inactivation of DnaA and supports translesion synthesis. It is a processivity factor, not a DNA polymerase or proofreading exonuclease.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003677 DNA binding | IDA PMID:10924523 The delta subunit of DNA polymerase III holoenzyme serves as... | ACCEPT | Summary: The beta clamp forms a topological ring around DNA and also contacts primed substrates. Reason: The beta clamp forms a topological ring around DNA and also contacts primed substrates. The broad DNA-binding claim is appropriate because both ssDNA-containing primer junctions and duplex DNA interact with the clamp. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: The beta clamp forms a topological ring around DNA and also contacts primed substrates. Reason: The beta clamp forms a topological ring around DNA and also contacts primed substrates. The broad DNA-binding claim is appropriate because both ssDNA-containing primer junctions and duplex DNA interact with the clamp. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0003887 DNA-directed DNA polymerase activity | IEA GO_REF:0000002 | REMOVE | Summary: The DNA-polymerizing reaction of the holoenzyme is performed by DnaE alpha. Reason: dnaN performs topological tethering and polymerase processivity; DNA polymerization is catalyzed by DnaE alpha. Holoenzyme nucleotide-incorporation assays and shared EC/Rhea labels do not establish that this individual subunit polymerizes DNA. Its actual molecular role is retained independently. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0005515 protein binding | IPI PMID:11525728 Mechanism of processivity clamp opening by the delta subunit... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P28630 from PMID:11525728. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14592985 Structural basis for recruitment of translesion DNA polymera... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:Q47155 from PMID:14592985. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15150238 Interaction of the sliding clamp beta-subunit and Hda, a Dna... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P69931 from PMID:15150238. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0A8E7 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0AC53 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0AFX0 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0AG07 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P69931 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P77395 from PMID:15690043. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16390442 Two processivity clamp interactions differentially alter the... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P04152 from PMID:16390442. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16546997 The beta sliding clamp binds to multiple sites within MutL a... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P23367, UniProtKB:P23909 from PMID:16546997. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19703395 Transposition into replicating DNA occurs through interactio... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P05845 from PMID:19703395. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19703395 Transposition into replicating DNA occurs through interactio... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P06710 from PMID:19703395. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19703395 Transposition into replicating DNA occurs through interactio... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P28630 from PMID:19703395. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:2040637 Mechanism of the sliding beta-clamp of DNA polymerase III ho... | MODIFY | Summary: The clamp–polymerase interaction tethers the polymerase to DNA and confers processivity; the specific regulator activity captures the demonstrated functional consequence. Reason: The clamp–polymerase interaction tethers the polymerase to DNA and confers processivity; the specific regulator activity captures the demonstrated functional consequence. Proposed replacements: DNA polymerase processivity factor activity Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0005515 protein binding | IPI PMID:21708944 DnaA protein DNA-binding domain binds to Hda protein to prom... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P69931 from PMID:21708944. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23435564 A direct proofreader-clamp interaction stabilizes the Pol II... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P03007 from PMID:23435564. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23435564 A direct proofreader-clamp interaction stabilizes the Pol II... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P10443 from PMID:23435564. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23549287 Architecture of the Pol III-clamp-exonuclease complex reveal... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P03007 from PMID:23549287. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23549287 Architecture of the Pol III-clamp-exonuclease complex reveal... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P10443 from PMID:23549287. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23549287 Architecture of the Pol III-clamp-exonuclease complex reveal... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:Q47155 from PMID:23549287. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23994470 A replicase clamp-binding dynamin-like protein promotes colo... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0DM85 from PMID:23994470. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P0AG07 from PMID:24561554. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P10443 from PMID:24561554. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P28630 from PMID:24561554. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P69931 from PMID:24561554. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26499492 cryo-EM structures of the E. coli replicative DNA polymerase... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P10443 from PMID:26499492. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7768937 Assembly of a chromosomal replication machine: two DNA polym... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P06710 from PMID:7768937. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7768937 Assembly of a chromosomal replication machine: two DNA polym... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P28630 from PMID:7768937. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9545254 Devoted to the lagging strand-the subunit of DNA polymerase ... | REMOVE | Summary: The reported interaction does not specify a useful molecular function. Reason: This row reports binding of dnaN to UniProtKB:P10443 from PMID:9545254. Bare protein binding is uninformative under the project policy; removing the annotation does not deny the interaction. A partner list alone does not justify transferring the partner’s catalytic activity. Source availability and the distinction between focused interaction assays and large-scale screens are recorded in the reference notes. Supporting Evidence: |
| GO:0005737 cytoplasm | EXP PMID:23994470 A replicase clamp-binding dynamin-like protein promotes colo... | MODIFY | Summary: The soluble protein acts in the cytosolic replication machinery; cytosol is a supported refinement of the broad cytoplasm annotation.. Reason: The soluble protein acts in the cytosolic replication machinery; cytosol is a supported refinement of the broad cytoplasm annotation. Proposed replacements: cytosol Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: The soluble protein acts in the cytosolic replication machinery; cytosol is a supported refinement of the broad cytoplasm annotation.. Reason: The soluble protein acts in the cytosolic replication machinery; cytosol is a supported refinement of the broad cytoplasm annotation. Proposed replacements: cytosol Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0005829 cytosol | HDA PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona... | ACCEPT | Summary: The soluble chromosome-replication machinery acts in the bacterial cytosol. Reason: The soluble chromosome-replication machinery acts in the bacterial cytosol. The experimental localization annotation is consistent with the established protein architecture; a proteomics citation is not treated as a new single-protein microscopy experiment. Supporting Evidence: |
| GO:0005829 cytosol | IDA PMID:18304323 Protein abundance profiling of the Escherichia coli cytosol. | ACCEPT | Summary: The soluble chromosome-replication machinery acts in the bacterial cytosol. Reason: The soluble chromosome-replication machinery acts in the bacterial cytosol. The experimental localization annotation is consistent with the established protein architecture; a proteomics citation is not treated as a new single-protein microscopy experiment. Supporting Evidence: |
| GO:0006260 DNA replication | IEA GO_REF:0000002 | ACCEPT | Summary: dnaN directly participates in the chromosome-replication machinery through the activity described in its core function. Reason: dnaN directly performs topological tethering and polymerase processivity within the replication machinery. This supports participation in chromosome replication; the pathway-level term remains informative alongside the specific molecular function and subcomplex assignments. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0006261 DNA-templated DNA replication | NAS PMID:7574479 DNA polymerase III holoenzyme: structure and function of a c... | ACCEPT | Summary: dnaN directly participates in the chromosome-replication machinery through the activity described in its core function. Reason: dnaN directly performs topological tethering and polymerase processivity within the replication machinery. This supports participation in chromosome replication; the pathway-level term remains informative alongside the specific molecular function and subcomplex assignments. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0006271 DNA strand elongation involved in DNA replication | IBA GO_REF:0000033 | ACCEPT | Summary: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Reason: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Its structural contribution is part of replication, even though it does not incorporate nucleotides. PAINT lineage-loss inspection found no applicable IRD/IKR; the IBA is evaluated as an ancestral-function judgment, not by counting listed donors. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0006271 DNA strand elongation involved in DNA replication | IDA PMID:3519609 The beta subunit of the Escherichia coli DNA polymerase III ... | ACCEPT | Summary: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Reason: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Its structural contribution is part of replication, even though it does not incorporate nucleotides. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0006974 DNA damage response | IEP PMID:11967071 Over 1000 genes are involved in the DNA damage response of E... | UNDECIDED | Summary: The expression-screen annotation is compatible with DNA-damage regulation, but the exact dnaN expression result in the cited study has not been independently verified here. Reason: The expression-screen annotation is compatible with DNA-damage regulation, but the exact dnaN expression result in the cited study has not been independently verified here. Damage-tolerance functions do not alone establish this specific expression result. Supporting Evidence: |
| GO:0008408 3'-5' exonuclease activity | IEA GO_REF:0000002 | REMOVE | Summary: The electronic family mapping assigns the holoenzyme proofreading chemistry to a non-nuclease subunit. Reason: The electronic family mapping assigns the holoenzyme proofreading chemistry to a non-nuclease subunit. E. coli epsilon/DnaQ carries the 3′ to 5′ editing activity; the target instead performs its structurally distinct loader or sliding-clamp function. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0009360 DNA polymerase III complex | IDA PMID:3283127 DNA polymerase III holoenzyme of Escherichia coli. III. Dist... | MODIFY | Summary: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader.. Reason: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader. Proposed replacements: DNA polymerase processivity factor complex Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0009360 DNA polymerase III complex | IEA GO_REF:0000002 | MODIFY | Summary: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader.. Reason: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader. Proposed replacements: DNA polymerase processivity factor complex Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0009360 DNA polymerase III complex | NAS PMID:7574479 DNA polymerase III holoenzyme: structure and function of a c... | MODIFY | Summary: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader.. Reason: The beta dimer is the sliding-clamp subassembly of the Pol III holoenzyme, distinct from the catalytic core and the loader. Proposed replacements: DNA polymerase processivity factor complex Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0030174 regulation of DNA-templated DNA replication initiation | NAS PMID:21708944 DnaA protein DNA-binding domain binds to Hda protein to prom... | ACCEPT | Summary: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Reason: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Beta contributes the organizing platform, not DnaA ATPase chemistry. |
| GO:0030894 replisome | NAS PMID:31395754 A quest for coordination among activities at the replisome. | ACCEPT | Summary: The protein is a documented component of the E. Reason: The protein is a documented component of the E. coli replication machinery. Replisome membership is distinct from the smaller biochemical assemblies and does not mean every interaction is permanent. Supporting Evidence: |
| GO:0032297 negative regulation of DNA-templated DNA replication initiation | NAS PMID:28168278 Dynamic assembly of Hda and the sliding clamp in the regulat... | ACCEPT | Summary: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Reason: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Beta contributes the organizing platform, not DnaA ATPase chemistry. |
| GO:0042276 error-prone translesion synthesis | IMP PMID:15752198 Mutant forms of the Escherichia colibeta sliding clamp that ... | ACCEPT | Summary: Beta directly recruits and supports the translesion polymerase Pol V; separation-of-function clamp mutants distinguish this activity from ordinary Pol III replication. Reason: Beta directly recruits and supports the translesion polymerase Pol V; separation-of-function clamp mutants distinguish this activity from ordinary Pol III replication. Retain this genuine repair/tolerance role in the whole-gene review. Supporting Evidence: |
| GO:0042802 identical protein binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:1349852 Three-dimensional structure of the beta subunit of E. coli D... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:19834901 Benchmarking yeast two-hybrid systems using the interactions... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:23435564 A direct proofreader-clamp interaction stabilizes the Pol II... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042802 identical protein binding | IPI PMID:24627523 A second-generation protein-protein interaction network of H... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0042803 protein homodimerization activity | IDA PMID:3048397 The dimer of the beta subunit of Escherichia coli DNA polyme... | KEEP AS NON CORE | Summary: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Reason: Self-association is a real structural property of this protein, supported by its oligomeric assembly. Retain this precise interaction property as non-core; it is not a substitute for the functional activity of the assembled protein. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:0044787 bacterial-type DNA replication | IDA PMID:3283127 DNA polymerase III holoenzyme of Escherichia coli. III. Dist... | ACCEPT | Summary: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Reason: The beta sliding clamp directly supports processive chromosome-strand elongation by tethering DNA polymerase. Its structural contribution is part of replication, even though it does not incorporate nucleotides. Supporting Evidence: PMID:10924523 the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. |
| GO:1990078 replication inhibiting complex | IPI PMID:28168278 Dynamic assembly of Hda and the sliding clamp in the regulat... | ACCEPT | Summary: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Reason: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Beta contributes the organizing platform, not DnaA ATPase chemistry. |
| GO:1990085 Hda-beta clamp complex | IPI PMID:15150238 Interaction of the sliding clamp beta-subunit and Hda, a Dna... | ACCEPT | Summary: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Reason: DNA-loaded beta recruits Hda and participates in RIDA, which stimulates hydrolysis of DnaA-bound ATP and prevents inappropriate reinitiation. Beta contributes the organizing platform, not DnaA ATPase chemistry. |
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