AlgI is a multi-pass inner-membrane acyltransferase-family component of the alginate O-acetylation machinery. With AlgJ and AlgF it transfers an acetyl donor across or through the inner-membrane complex for subsequent addition to O-2 and O-3 positions of mannuronate residues in periplasmic alginate.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: AlgI is a multi-pass bacterial inner-membrane protein. Reason: The reviewed topology and membrane-bound acyltransferase-family assignment support this location. Supporting Evidence: file:PSEPK/algI/algI-uniprot.txt SUBCELLULAR LOCATION: Cell inner membrane |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: AlgI is the membrane-bound acyl-transfer component of the alginate O-acetylation complex. Reason: The exact donor and transient acceptor remain unresolved, so this broad valid term is preferable to assigning serine O-acetyltransferase or a fabricated substrate-specific activity. Supporting Evidence: file:PSEPK/algI/algI-uniprot.txt Belongs to the membrane-bound acyltransferase family |
| GO:0042121 alginic acid biosynthetic process | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: AlgI acts in post-polymerization alginate maturation rather than polymer formation itself. Reason: GO:0051979 is not an ontology descendant of GO:0042121, so replacing this row would lose its broader alginate-pathway context. The broad process is retained as non-core while the exact acetylation process is added separately; P. aeruginosa genetics show that algIJF are not required to synthesize the unacetylated polymer. Supporting Evidence: PMID:8636017 This indicated that the algIJF gene products were not required for polymer biosynthesis. |
| GO:0051979 alginic acid acetylation | ISS PMID:12003941 Mutant analysis and cellular localization of the AlgI, AlgJ,... | NEW | Summary: AlgI is required for transfer of acetyl groups into the alginate O-acetylation machinery. Reason: Isogenic P. aeruginosa algI deletion and complementation establish the ortholog role, and Q88ND2 retains the exact AlgI family, topology, and syntenic operon position. Supporting Evidence: PMID:12003941 defined nonpolar algI, algJ, and algF deletion mutants of P. aeruginosa strain FRD1 were constructed, and each mutant produced alginate lacking O-acetyl groups. |
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Download this section (compressed HTML)Q: What is the immediate acetyl donor and acceptor handled by KT2440 AlgI within the AlgI-AlgJ-AlgF complex?
Experiment: Reconstitute AlgI with AlgJ and AlgF in proteoliposomes and trace transfer from isotopically labeled acetyl donors.
Type: membrane-complex reconstitution
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