rpoC (PP_0448) encodes the beta-prime subunit of the bacterial DNA-directed RNA polymerase core enzyme. RpoC pairs with the beta subunit RpoB to form the catalytic cleft of the alpha2-beta-beta-prime-omega RNAP core, coordinating divalent metal ions and nucleic-acid contacts needed for DNA-templated RNA synthesis. Its core role is contribution to complex-level RNA polymerase activity, with magnesium and zinc binding as important subunit-specific features.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000287 magnesium ion binding | IEA GO_REF:0000104 | ACCEPT | Summary: Magnesium ion binding is appropriate for the beta-prime subunit active center architecture. Reason: UniProt records Mg(2+) as a cofactor for the RpoC subunit, consistent with the conserved RNAP catalytic mechanism. Supporting Evidence: file:PSEPK/rpoC/rpoC-uniprot.txt Binds 1 Mg(2+) ion per subunit. |
| GO:0003677 DNA binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: DNA binding is plausible for the beta-prime subunit within the RNAP cleft, but it is a broad supporting activity. Reason: Retain as non-core context. Complex-level DNA-directed RNA polymerase activity and metal-binding features better capture the main role. |
| GO:0003899 DNA-directed RNA polymerase activity | IEA GO_REF:0000120 | ACCEPT | Summary: RpoC is an essential beta-prime subunit of the bacterial RNAP active-center cleft, but RNA synthesis is performed by the assembled core enzyme. Reason: RpoC carries the conserved metal-binding active-center architecture and directly participates in nucleotide addition by the assembled core. Retain the annotation while the synthesis records contribution to the complex-level function rather than activity by isolated RpoC. Supporting Evidence: file:PSEPK/rpoC/rpoC-uniprot.txt DNA-dependent RNA polymerase catalyzes the transcription of |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: Cytosolic localization is appropriate for a soluble bacterial RNA polymerase core subunit. Reason: RpoC functions in the bacterial cytosol/nucleoid as part of the transcription machinery. |
| GO:0006351 DNA-templated transcription | IEA GO_REF:0000120 | ACCEPT | Summary: RpoC directly participates in DNA-templated transcription as an essential beta-prime subunit of bacterial RNA polymerase. Reason: Correct process annotation for a core RNAP subunit. |
| GO:0008270 zinc ion binding | IEA GO_REF:0000104 | ACCEPT | Summary: Zinc ion binding is appropriate for the beta-prime subunit, which UniProt annotates as binding two Zn(2+) ions per subunit. Reason: Retain as a subunit-specific cofactor/structural feature of RpoC. Supporting Evidence: file:PSEPK/rpoC/rpoC-uniprot.txt Binds 2 Zn(2+) ions per subunit. |
| GO:0034062 5'-3' RNA polymerase activity | IEA GO_REF:0000116 | ACCEPT | Summary: The Rhea-derived polymerase activity reflects RNA-chain extension by the assembled RNAP core. Reason: RpoC is a required catalytic-cleft subunit whose metal-binding active center directly participates in 5'-3' RNA-chain extension by the assembled core. This is retained as a catalytic-subunit function, not a claim about isolated RpoC. Supporting Evidence: file:PSEPK/rpoC/rpoC-uniprot.txt DNA-dependent RNA polymerase catalyzes the transcription of |
| GO:0000428 DNA-directed RNA polymerase complex | ISS file:PSEPK/rpoC/rpoC-uniprot.txt | NEW | Summary: RpoC is part of the bacterial DNA-directed RNA polymerase core complex. Reason: UniProt records Q88QP1 as the beta-prime subunit in the alpha2-beta- beta-prime-omega RNAP catalytic core, so explicit complex membership is useful for interpreting the complex-level polymerase MF. Supporting Evidence: file:PSEPK/rpoC/rpoC-uniprot.txt The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' file:PSEPK/rpoC/rpoC-deep-research-openscientist.md is therefore the capstone subunit whose correct incorporation completes the catalytically competent core. |
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Download this section (compressed HTML)Q: Should UniProt-derived DNA-directed RNA polymerase activity on bacterial core subunits be represented with contributes_to semantics in downstream GO curation, or retained as direct enables by current UniProt convention?
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Download this section (compressed HTML)Reviewed every existing GOA-derived row and the proposed complex membership
row against Q88QP1 UniProt/HAMAP evidence and the completed OpenScientist gene
report. Magnesium and zinc binding, cytosol, transcription, and complex
membership are retained; broad DNA binding remains non-core. GO:0003899 and
GO:0034062 are accepted because RpoC supplies the metal-binding active-center
architecture and directly participates in catalysis. Core-function synthesis
still records this as a contribution to activity of the assembled core rather
than activity by isolated RpoC.
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