GO_REF:0000041

Gene Ontology annotation based on UniPathway vocabulary mapping

UniPathway mapping supplies the alginic acid biosynthetic process annotation.

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping

UniProt subcellular-location mapping supplies the cell outer membrane annotation.

file:PSEPK/algK/algK-uniprot.txt

UniProtKB reviewed entry for algK

UniProt describes AlgK as an AlgK-family outer-membrane/periplasmic-side protein involved in alginate biosynthesis.

file:PSEPK/algK/algK-goa.tsv

QuickGO GOA annotations for algK

The fetched GOA table contains the annotations reviewed for algK.

file:interpro/panther/PTHR11102/PTHR11102-metadata.yaml

PANTHER family metadata for algK

The PANTHER family assignment is broad and not used as primary evidence because the reviewed UniProt entry provides the alginate-specific function.

file:PSEPK/algK/algK-deep-research-falcon.md

Falcon (Edison Scientific) deep research report on algK (Q88NC7 / PP_1285) in Pseudomonas putida KT2440

AlgK is an outer-membrane-anchored periplasmic TPR/Sel1-like repeat scaffold protein required for alginate export.

"AlgK is an outer-membrane (OM)–anchored, periplasmic TPR/Sel1-like repeat protein"
AlgK is a non-catalytic assembly/scaffolding factor, not an enzyme; it is essential for efficient alginate polymer production and export.

"AlgK is not an enzyme catalyzing a chemical reaction; rather, it is a **non-catalytic assembly/scaffolding factor** essential for efficient alginate polymer production and export."
AlgK connects the OM export channel AlgE with periplasmic modifying enzyme AlgX and the inner-membrane polymerization components Alg8/Alg44.

"connects the OM export channel (AlgE) with periplasmic modifying enzymes (notably AlgX) and IM polymerization components (Alg8/Alg44)"
A 2.5 A crystal structure of the AlgK-AlgX complex was solved using P. putida proteins, providing direct P. putida evidence for the AlgK-AlgX scaffold interface.

"a **2.5 Å crystal structure of the AlgK–AlgX complex** was solved using the *Pseudomonas putida* proteins, defining a direct interface (AlgX N-terminus with AlgK TPRs 9–10)"
AlgK is tethered to the outer membrane via N-terminal lipidation, confirmed by in vivo palmitate labeling and outer-membrane fractionation in P. aeruginosa.

"in vivo lipidation** was confirmed by palmitate labeling, - AlgK localized to **outer-membrane–enriched fractions** by sucrose-gradient fractionation,"
Loss of algK causes AlgE mislocalization, indicating AlgK positions/stabilizes the AlgE export porin in the secretion machinery.

"algK deletion caused **AlgE mislocalization** to both inner and outer membrane fractions instead of being exclusively OM-localized"
algK deletion mutants fail to export high-molecular-weight alginate and instead secrete low-molecular-weight uronic acids (AlgL degradation products).

"ΔalgK mutants fail to export high-molecular-weight alginate** and instead show secretion of **low-molecular-weight uronic acids**"
No KT2440 (PP_1285/Q88NC7)-specific wet-lab paper was retrieved; KT2440 function is inferred by orthology from the conserved AlgK family.

"no KT2440 (PP_1285/Q88NC7)-specific wet-lab paper** was retrieved"