PP_2634

UniProt ID: Q88JL5
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
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Gene Description

PP_2634 is a predicted BcsQ-family accessory protein of the Pseudomonas putida KT2440 cellulose biosynthesis machinery. BcsQ and P-loop NTPase family signatures support a role in assembly or stabilization of the synthase complex. Characterized E. coli BcsQ contacts the BcsA PilZ domain and associates with BcsR and BcsE. The KT2440 protein has a divergent N-terminal nucleotide-binding region, and its nucleotide specificity, hydrolytic activity, partners and localization remain untested.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0090540 bacterial cellulose biosynthetic process
ISS
PMID:19400787
BcsQ is an essential component of the Escherichia coli cellu...
NEW
Summary: Retain the inherited proposed cellulose biosynthesis annotation for the BcsQ-family structural accessory protein.
Reason: The inherited NEW assertion is retained. Target-specific BcsQ family signatures and bcs-locus context link PP_2634 to characterized BcsQ. Beyond knockout necessity, the E. coli macrocomplex structure places BcsQ against the synthase PilZ domain, consistent with direct structural participation by stabilizing an active assembly. Transfer supports the biosynthetic role without asserting cellulose polymerase chemistry, polar localization, or ATP-driven transport for KT2440. The exact target nucleotide cycle and partner set remain untested. GO:0090540 adds bacterial context to the same cellulose-forming chemistry; it does not impose a native-output, intact-cell, crystallinity or fibril criterion. The inferred participation is structural support of a bacterial cellulose-synthase assembly; target nucleotide cycling and native output remain untested.
Supporting Evidence:
file:PSEPK/PP_2634/PP_2634-uniprot.txt
DR InterPro; IPR017746; Cellulose_synthase_operon_BcsQ.
PMID:39394223
BcsQ buttresses the PilZ domain, likely stabilizing the catalytically competent state.
PMID:19400787
we show that yhjQ, but not yhjR, is essential for cellulose biosynthesis; it has therefore been renamed bcsQ

Core Functions

Predicted BcsQ-family structural contribution to cellulose synthase assembly or stabilization, inferred from target BcsQ signatures and the E. coli BcsQ-synthase interface. No specific molecular-function term is asserted because the target nucleotide activity and exact partner-dependent mechanism remain unresolved.

Supporting Evidence:
  • file:PSEPK/PP_2634/PP_2634-uniprot.txt
    DR InterPro; IPR017746; Cellulose_synthase_operon_BcsQ.
  • PMID:39394223
    BcsQ buttresses the PilZ domain, likely stabilizing the catalytically competent state.
  • PMID:19400787
    we show that yhjQ, but not yhjR, is essential for cellulose biosynthesis; it has therefore been renamed bcsQ

References

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Suggested Questions for Experts

Q: Should UniProt update PP_2634's submitted/display name from "Cellulose synthase" to BcsQ or cellulose biosynthesis protein BcsQ?

Q: Does KT2440 PP_2634 localize the cellulose synthase machinery to a specific subcellular site as shown for enterobacterial BcsQ?

Q: Does the divergent KT2440 BcsQ nucleotide-binding region bind or hydrolyze ATP, and which partners activate or stabilize its nucleotide-loaded state?

Suggested Experiments

Experiment: Delete PP_2634 in KT2440, complement with wild-type and Walker-A mutant variants, and assay cellulose production and biofilm/rhizosphere phenotypes.

Type: targeted genetics and cellulose phenotype assay

Experiment: Express a functional fluorescent PP_2634/BcsQ fusion and image localization relative to BcsA/BcsB and sites of cellulose deposition.

Type: live-cell localization assay

Deep Research

OpenScientist

(PP_2634-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(PP_2634-notes.md)

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