This record represents full-length, functional BcsQ, including the repaired K-12 allele in strain AR3110. BcsQ is a cytosolic SIMIBI-family nucleotide-binding accessory protein that associates with BcsR, BcsE and cellulose synthase, helping stabilize the active assembly. The close strain 1094 allele forms ATP-loaded BcsRQ dimers and exhibits weak, regulated ATP hydrolysis in vitro. The precise coupling of hydrolysis to cellulose production remains unresolved. The native K-12 downstream-start pseudogene prediction is represented separately by P37655.
The preferred accession for this review is P0DP92. These relationships are manually assessed.
REFERENCE PROTEOME LOCUS COUNTERPART · Reviewed 2026-11-06
Reference proteome: UP000000625
Same bcsQ locus with distinct record integrity: P0DP92 is the functional full-length/repaired product, while P37655 is the downstream-start native K-12 pseudogene prediction. The relationship does not assert sequence or functional equivalence and does not transfer ATP activity or localization automatically.
The preserved fragment record explicitly belongs to the K-12 reference proteome.
file:ECOLI/bcsQ__P37655/bcsQ__P37655-uniprot.txt
DR Proteomes; UP000000625; Chromosome.
The UniProt fragment record explicitly points to the intact P0DP92 protein upon reading-frame repair.
file:ECOLI/bcsQ__P37655/bcsQ__P37655-uniprot.txt
When the reading frame is restored cellulose CC biosynthesis is also restored, see (AC P0DP92) for an intact protein.
The 242-residue fragment differs by loss of the full-length N-terminal segment and a downstream initiator methionine; its remaining 241 residues exactly match the intact record.
file:ECOLI/bcsQ/bcsQ-source-analysis/README.md
P37655 residues 2-242 exactly match P0DP92 residues 10-250.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | EXP PMID:19400787 BcsQ is an essential component of the Escherichia coli cellu... | MODIFY | Summary: Refine the broad cytoplasmic location to the cytoplasmic face of the synthase-containing membrane. Reason: The curator-backed cytoplasmic location is sound. Full-length BcsQ acts on the cytosolic face of the inner-membrane synthase in characterized assemblies. The structural evidence uses the close 1094 allele, not the K-12 fragment; it supports the activity-associated membrane-side localization while allowing soluble unassembled BcsQ. No integral-membrane topology is claimed. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:39394223 BcsQ buttresses the PilZ domain, likely stabilizing the catalytically competent state. file:ECOLI/bcsQ/bcsQ-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Refine the broad cytoplasmic location to the cytoplasmic face of the synthase-containing membrane. Reason: The curator-backed cytoplasmic location is sound. Full-length BcsQ acts on the cytosolic face of the inner-membrane synthase in characterized assemblies. The structural evidence uses the close 1094 allele, not the K-12 fragment; it supports the activity-associated membrane-side localization while allowing soluble unassembled BcsQ. No integral-membrane topology is claimed. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:39394223 BcsQ buttresses the PilZ domain, likely stabilizing the catalytically competent state. file:ECOLI/bcsQ/bcsQ-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005524 ATP binding | ISS PMID:33563593 Architecture and regulation of an enterobacterial cellulose ... | NEW | Summary: ATP binding stabilizes the functional BcsRQ assembly. Reason: ATP binding stabilizes the functional BcsRQ assembly. The structurally characterized 1094 allele differs from the repaired K-12 sequence at residue 249 (A to K), so its ATP-bound structures provide close-allele inference rather than an identical-sequence assay. This does not assert a strong ATPase motor. Supporting Evidence: PMID:33563593 BcsRQ crystallized as ATP-bound “sandwich” or “tango” dimers of heterodimers. file:ECOLI/bcsQ/bcsQ-uniprot.txt A -> K (in strain: 1094) |
| GO:0090540 bacterial cellulose biosynthetic process | IC PMID:24097954 Cellulose as an architectural element in spatially structure... | NEW | Summary: Full-length BcsQ participates in cellulose production by supporting the active synthase assembly. Reason: Full-length BcsQ participates in cellulose production by supporting the active synthase assembly. Repaired K-12 genetics establish pathway relevance and 1094 structures show the protein itself buttressing BcsA, providing structural participation beyond deletion necessity. No process term is added to the native pseudogene fragment. Same-role BcsQ comparators Q8Z292, Q8ZLB6 and Q88JL5 lack this process annotation in the checked QuickGO snapshot. That absence is not used to argue a gap; the proposal is based on direct structural participation by BcsQ plus K-12 repair genetics, with no matching existing GO-CAM role found in the local index. Supporting Evidence: PMID:24097954 For changing codon 6 of bcsQ from TAG(stop) to TTG(leucine) in the chromosomal copy of bcsQ in strain W3110 PMID:39394223 BcsQ buttresses the PilZ domain, likely stabilizing the catalytically competent state. |
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Experiment: Compare matched native and recombinant backgrounds while measuring cellulose synthesis and secretion separately; include allele/construct controls for the activity under study.
Type: controlled genetic and biochemical comparison
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