celB

Summary: Retain membrane-anchored cellulose synthase partner localization.

Reason: The target has a signal peptide and C-terminal membrane helix, the specific AcsB/BcsB family assignment, and a curated RuleBase inner-membrane location. The homolog structure independently establishes membrane-anchored periplasmic BcsB architecture.

Summary: Replace donor-centric metabolism with the cellulose biosynthetic role.

Reason: CelB is a structural component of cellulose synthase; CelA performs UDP-glucose glycosyl transfer. BcsB-specific domains and the homolog BcsAB structure support direct participation by organizing the synthesis complex, independently of mutant necessity. GO:0030244 lies under glucan/polysaccharide biosynthesis. It is not a descendant of UDP-glucose metabolism: this is an explicit role correction, not a claimed hierarchical refinement. Same-role QuickGO checks on E. coli P37652 and P. putida Q88JL3 found the same broad donor-metabolism annotation and no cellulose-biosynthesis row. That absence is not evidence of a gap; the replacement rests on structural participation and the conserved family, not on annotation counting. No duplicate NEW process row is added, and no target GO-CAM was present in the index. Use the bacterial-context subtype GO:0090540 of cellulose biosynthesis; the term adds no new native-output or fibril criterion. CelB contributes structural support to a bacterial synthase; this is a role correction from donor metabolism, not assignment of CelA catalysis.

Proposed replacements: bacterial cellulose biosynthetic process

Summary: Refine membrane to plasma membrane.

Reason: The target signal peptide and C-terminal membrane anchor, together with conserved BcsB structure, identify the inner membrane. Plasma membrane is a checked descendant already present in this review.

Proposed replacements: plasma membrane