GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:PSEPK/algJ/algJ-uniprot.txt

UniProtKB reviewed entry for algJ (Q88ND3)

The record assigns the AlgJ family, SGNH-like architecture, periplasmic membrane association, and alginate O-acetylation role.

file:PSEPK/algJ/algJ-goa.tsv

QuickGO GOA annotations for algJ

The fetched GOA table contains the three annotations reviewed here.

PMID:12003941

Mutant analysis and cellular localization of the AlgI, AlgJ, and AlgF proteins required for O acetylation of alginate in Pseudomonas aeruginosa.

Nonpolar algJ deletion abolishes O-acetylation, complementation restores it, and localization experiments place AlgJ on the periplasmic face of the inner membrane.

PMID:8636017

Identification of algI and algJ in the Pseudomonas aeruginosa alginate biosynthetic gene cluster which are required for alginate O acetylation.

Genetic analysis separates AlgJ-dependent acetylation from polymer synthesis and C5 epimerization.

PMID:25165982

P. aeruginosa SGNH hydrolase-like proteins AlgJ and AlgX have similar topology but separate and distinct roles in alginate acetylation.

The study solves the KT2440 Q88ND3 soluble-domain structure and distinguishes in-vitro acetylesterase activity from the unresolved in-vivo relay role.

PMID:31900562

Analysis of the alginate O-acetylation machinery in Pseudomonas aeruginosa.

AlgJ interacts with AlgI and AlgF in the O-acetylation complex, but AlgJ and AlgX do not mutually determine stability.

file:projects/P_PUTIDA/deep-research/PSEPK__alginate-o-acetylation__ppu00543-deep-research-openscientist.md

OpenScientist PSEPK alginate O-acetylation synthesis

The report distinguishes the AlgJ SGNH relay role from the terminal polymer O-acetyltransferase role of AlgX.

file:modules/alginate_o_acetylation.yaml

Alginate O-acetylation module

AlgJ implements the periplasm-facing acetyl-relay part.