Alginate O-acetylation

Bacterial alginate O-acetylation modifies mannuronate residues as the polymer traverses the cell envelope. In characterized pseudomonads, the membrane MBOAT component AlgI and periplasm-facing SGNH protein AlgJ act with the interaction mediator AlgF and polymer-modifying enzyme AlgX. Azotobacter uses homologous proteins, with AlgV corresponding to Pseudomonas AlgJ. AlgX directly transfers acetyl groups to polymannuronate in vitro, while the physiological donor and complete AlgI-to-AlgJ-to-AlgX relay remain unresolved. Polymer precursor synthesis, polymerization, export and mannuronate epimerization are separate but physically coupled processes.

MODULE:alginate_o_acetylationCOMPLETEABSTRACTBiological Processmodules/alginate_o_acetylation.yaml
alginic acid acetylationGO:0051979
PMID:40171682
Comparative transmembrane acylation review defines the proposed relay and its unresolved steps.
PMID:40821665
Comparative Azotobacter review provides nomenclature and physiological scope, with mechanistic generalizations checked against primary studies.
PMID:37797696
Direct interaction and structural work identifies a noncatalytic role for AlgF.
PMID:25165982
Direct AlgJ/AlgX biochemistry separates esterase assays from polymer transfer.
PMID:10352233
Native Azotobacter algF mutation establishes an acetylation role outside Pseudomonas.

The review integrates direct target biochemistry, native genetics and explicit homology inference. Scope is ABSTRACT and generalized to the Pseudomonas and Azotobacter lineages that carry the algIJFX (algIVFX) genes, with P. aeruginosa as the experimental reference, P. putida KT2440 as the second Pseudomonas exemplar and A. vinelandii as the cross-genus exemplar supported by a native algF mutant; no further organisms are added without target evidence. All four roles have family descriptors and verified exemplars. InterPro AlgI/AlgF family entries and AlgJ/AlgX domain entries are the descriptor term ids (every representative carries them); their labels are the InterPro short names quoted from the representatives' UniProt DR lines, since InterPro is not label-validated by the ontology adapters. AlgI is the only member with a PANTHER family, PTHR13285 (official label ACYLTRANSFERASE), reviewed in interpro/panther/PTHR13285/PTHR13285-review.yaml; it is too broad to be the AlgI family term, and its SF23 subfamily (TEICHOIC ACID D-ALANYLTRANSFERASE) mixes DltB, PatA and AlgI, so neither is asserted and its label is not evidence of AlgI substrate specificity. The family-root PAINT node supports only the broad acyltransferase activity asserted here. AlgF is not assigned intrinsic acetyltransferase activity solely because it is required for acetylation. GO:0051979 is not a descendant of GO:0042121; modification and polymer biosynthesis/export are distinct roles. The lack of a substrate-specific AlgX GO term is an ontology note, not an unknown biological mechanism. New provider requests failed; manually inspected primary literature and genuine existing reports are documented in the notes.

5Nodes
4Parts
0Variant Sets
0Variants
4Annotons
4Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:alginate_o_acetylation deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ representative grounding skipped for abstract module.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Function consistency and core coverage

6 gene-function check(s) reflected in core functions · 0 conflict(s) · 2 evidence or coverage gap(s) (8 comparison(s))

Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.

AnnotonParticipantFunctionAssessment
algI_acyltransferase_activity algI (Pseudomonas putida KT2440)
UniProtKB:Q88ND2
Family Representative
acyltransferase activity
GO:0016746
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algI_acyltransferase_activity algI (Pseudomonas aeruginosa)
UniProtKB:Q51392
Family Representative
acyltransferase activity
GO:0016746
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algI_acyltransferase_activity algI (Azotobacter vinelandii ATCC 9046)
UniProtKB:O52196
Family Representative
acyltransferase activity
GO:0016746
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algX_o_acetyltransferase_activity algX (Pseudomonas putida KT2440)
UniProtKB:Q88ND0
Family Representative
O-acetyltransferase activity
GO:0016413
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algX_o_acetyltransferase_activity algX (Pseudomonas aeruginosa)
UniProtKB:Q51372
Family Representative
O-acetyltransferase activity
GO:0016413
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algX_o_acetyltransferase_activity algX (Azotobacter vinelandii ATCC 9046)
UniProtKB:O52194
Family Representative
O-acetyltransferase activity
GO:0016413
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
algI_acyltransferase_activity AlgI family
InterPro:IPR028362
Family
acyltransferase activity
GO:0016746
Family Review Missing
No supported structured family review is available for InterPro:IPR028362.
algX_o_acetyltransferase_activity AlgX polymer-modification and export-associated family
Family
O-acetyltransferase activity
GO:0016413
Family Id Missing
The family has no identifier linking it to a curated family review.

Gene-review completeness (12/12 grounded genes reviewed)

12 complete review(s) · 1 with deep research · 0 missing review · 11 reviewed but lacking deep research

Gene Review Complete Deep research
algF P70799 ✓ ✓ ✗
algF Q06062 ✓ ✓ ✗
algF Q88ND4 ✓ ✓ ✓
algI O52196 ✓ ✓ ✗
algI Q51392 ✓ ✓ ✗
algI Q88ND2 ✓ ✓ ✗
algJ Q51393 ✓ ✓ ✗
algJ Q88ND3 ✓ ✓ ✗
algV O52197 ✓ ✓ ✗
algX O52194 ✓ ✓ ✗
algX Q51372 ✓ ✓ ✗
algX Q88ND0 ✓ ✓ ✗

Details

Context
Pseudomonas and Azotobacter alginate-acetylating lineagesNCBITaxon:135621
PMID:40171682
Review places alginate acetylation in selected Pseudomonas and Azotobacter lineages and distinguishes the proposed MBOAT/SGNH relay from experiments on other polymers.
PMID:40821665
Comparative Azotobacter review identifies the AlgI/AlgV/AlgF/AlgX implementation; its categorical donor and enzyme descriptions are qualified by primary evidence.
PMID:10352233
A native Azotobacter nonpolar algF mutant produces unacetylated alginate, supporting cross-genus process conservation.

Brown-algal alginate production and other bacterial surface-polymer acylation systems do not establish this module. Current selected native proteins span P. aeruginosa PAO1-derived experiments, P. putida KT2440 and A. vinelandii ATCC 9046.

Alginate O-acetylationBiological Processalginate_o_acetylation

Four complementary roles in alginate acetylation; part ordering is presentational and does not establish a linear sequence of four catalytic reactions.

alginic acid acetylationGO:0051979
Context
Pseudomonas and Azotobacter alginate-acetylating lineagesNCBITaxon:135621
PMID:40171682
Review places alginate acetylation in selected Pseudomonas and Azotobacter lineages and distinguishes the proposed MBOAT/SGNH relay from experiments on other polymers.
PMID:40821665
Comparative Azotobacter review identifies the AlgI/AlgV/AlgF/AlgX implementation; its categorical donor and enzyme descriptions are qualified by primary evidence.
PMID:10352233
A native Azotobacter nonpolar algF mutant produces unacetylated alginate, supporting cross-genus process conservation.

Brown-algal alginate production and other bacterial surface-polymer acylation systems do not establish this module. Current selected native proteins span P. aeruginosa PAO1-derived experiments, P. putida KT2440 and A. vinelandii ATCC 9046.

Connections

algI_membrane_transfer -> algJ_relay Provides Input For
Proposed acetyl delivery from AlgI to the periplasmic AlgJ/AlgV component; native association is demonstrated for Pa, but the chemical intermediate is not.
PMID:37797696
Pa AlgI and AlgJ associate in native co-immunoprecipitation experiments.
PMID:40171682
The full AlgI-to-AlgJ acyl-shuttle model remains experimentally incomplete.
algJ_relay -> algX_polymer_transfer Provides Input For
Proposed acetyl handoff to AlgX; the physiological AlgJ donor/acceptor pair and direct transfer remain unresolved.
PMID:25165982
AlgJ and AlgX have distinct biochemical roles; only AlgX directly modifies the tested polymer.
PMID:40171682
The review identifies AlgJ-to-AlgX handoff as the major unresolved mechanistic step.
algF_accessory -> algJ_relay Provides Input For
Provides interaction/assembly context, not an asserted acetyl substrate. Pairwise binding supports this model; simultaneous bridging is not established.
PMID:37797696
Direct KT2440 pairwise AlgF interactions and Pa AlgF-AlgX association support organization of the acetylation machinery.
algF_accessory -> algX_polymer_transfer Provides Input For
Provides interaction/assembly context, not an asserted acetyl substrate. Pairwise binding supports this model; simultaneous bridging is not established.
PMID:37797696
Direct KT2440 pairwise AlgF interactions and Pa AlgF-AlgX association support organization of the acetylation machinery.
Part 1: inner-membrane acetyl-donor transfer
AlgI membrane acetyl-transfer componentReactionalgI_membrane_transfer

Annotons

AlgI membrane acyltransferase
algI_acyltransferase_activity
Participant: Family: AlgI family
Family:
AlgI familyInterPro:IPR028362
Representative Members: algI (Pseudomonas putida KT2440)UniProtKB:Q88ND2 algI (Pseudomonas aeruginosa)UniProtKB:Q51392 algI (Azotobacter vinelandii ATCC 9046)UniProtKB:O52196
Required Function:
acyltransferase activityGO:0016746

Function

acyltransferase activityGO:0016746

Processes

alginic acid acetylationGO:0051979

Locations

plasma membraneGO:0005886

Multipass membrane component required for acetylation. MBOAT ancestry supports an acyltransferase role, but neither the immediate physiological donor nor the complete target-specific covalent relay has been experimentally reconstructed. The proposed C-terminal acyl-shuttle mechanism is informed by Dlt and PatA systems rather than demonstrated AlgI chemistry.

PMID:12003941
Nonpolar mutants lose alginate O-acetylation; topology places AlgI across the inner membrane.
PMID:31900562
Mutant complementation and stability studies connect AlgI to the acetylation complex; the accessible record supports this at abstract level.
PMID:37797696
Native P. aeruginosa co-immunoprecipitation supports AlgI association with AlgJ.
PMID:40171682
Review explicitly qualifies the complete proposed alginate acyl-shuttle model.
Part 2: periplasm-facing acetyl relay
AlgJ/AlgV SGNH relay componentReactionalgJ_relay

Annotons

AlgJ/AlgV periplasm-facing acetylation component
algJ_relay_role
Participant: Family: AlgJ/AlgV SGNH acetylation-component family
Family:
AlgJ/AlgV SGNH acetylation-component family The ortholog group is represented by verified proteins. The specific InterPro domain is recorded separately as required_domain, rather than mislabeled as a full-length family identifier. In Azotobacter the acetylation homolog is called AlgV; a separate historical AlgJ designation names the export protein and is excluded.
Representative Members: algJ (Pseudomonas putida KT2440)UniProtKB:Q88ND3 algJ (Pseudomonas aeruginosa)UniProtKB:Q51393 algV (Azotobacter vinelandii ATCC 9046)UniProtKB:O52197
Required Domain:
Alginate O-acetyltranferase AlgJInterPro:IPR034657

Processes

alginic acid acetylationGO:0051979

Locations

plasma membraneGO:0005886 periplasmic spaceGO:0042597

Membrane-associated periplasmic SGNH protein required for alginate acetylation. P. putida and P. aeruginosa AlgJ have directly measured acetylesterase activity with artificial substrates; the physiological relay substrate and transfer to AlgX remain unresolved. The module therefore records the proposed contribution without equating in-vitro hydrolysis with the native reaction.

PMID:25165982
Both Pseudomonas AlgJ proteins have measured acetylesterase activity. Pa AlgJ has weak or undetectable polymer binding; direct polymer acetyl transfer was demonstrated for AlgX and was not established for AlgJ.
AlgJ exhibits acetylesterase activity in vitro.
PMID:37797696
KT2440 AlgF-AlgJ binding is directly measured by ITC; Pa native AlgI-AlgJ association supports complex organization.
PMID:10352233
Azotobacter algV is sequenced in the native alginate locus; this is not a purified AlgV assay.
Part 3: periplasmic accessory support
AlgF periplasmic accessory componentBiological ProcessalgF_accessory

Annotons

AlgF accessory protein
algF_accessory_role
Participant: Family: AlgF family
Family:
AlgF familyInterPro:IPR035422
Representative Members: algF (Pseudomonas putida KT2440)UniProtKB:Q88ND4 algF (Pseudomonas aeruginosa)UniProtKB:Q06062 algF (Azotobacter vinelandii ATCC 9046)UniProtKB:P70799

Processes

alginic acid acetylationGO:0051979

Locations

periplasmic spaceGO:0042597

Periplasmic noncatalytic component. KT2440 AlgF binds AlgJ and AlgX in separate in-vitro assays and lacks detected acetylesterase activity; P. aeruginosa AlgF has native AlgX association and no detected isolated polymannuronate binding. These support an interaction-mediator model, but simultaneous ternary bridging and exact acetyl-relay geometry remain proposed. Native Azotobacter algF genetics supports participation without establishing its molecular interaction mechanism.

PMID:37797696
Target-specific structural, binding and association studies support an interaction role, with the Pseudomonas species and constructs distinguished.
PMID:31900562
AlgF deletion affects acetylation and production/stability in the studied P. aeruginosa background.
PMID:10352233
The Azotobacter nonpolar algF mutant produces unacetylated alginate.
As expected, AJ34 produced unacetylated alginate.
Part 4: terminal polymer O-acetylation
AlgX alginate O-acetyltransferaseReactionalgX_polymer_transfer

Annotons

AlgX terminal O-acetyltransferase
algX_o_acetyltransferase_activity
Participant: Family: AlgX polymer-modification and export-associated family
Family:
AlgX polymer-modification and export-associated family The ortholog group is represented by verified proteins. The specific InterPro domain is recorded separately as required_domain, rather than mislabeled as a full-length family identifier. Characterized full-length members also contain an AlgX C-terminal carbohydrate-binding module (InterPro:IPR031798); the N-terminal signature alone does not prove polymer binding or the full activity.
Representative Members: algX (Pseudomonas putida KT2440)UniProtKB:Q88ND0 algX (Pseudomonas aeruginosa)UniProtKB:Q51372 algX (Azotobacter vinelandii ATCC 9046)UniProtKB:O52194
Required Function:
O-acetyltransferase activityGO:0016413
Required Domain:
Alginate biosynthesis protein AlgX, N-terminalInterPro:IPR034655

Function

O-acetyltransferase activityGO:0016413
Substrates: unacetylated mannuronate residues in alginate
Products: O-acetylated mannuronate residues in alginate

Processes

alginic acid acetylationGO:0051979

Locations

periplasmic spaceGO:0042597

Terminal polymer-modifying enzyme. P. aeruginosa AlgX directly transfers acetyl groups from an artificial donor to polymannuronate; its catalytic-site mutants secrete nonacetylated polymer. KT2440 AlgX has directly measured acetylesterase activity, polymer binding and an AlgK-complex structure; polymer acetyl transfer is inferred from the characterized homolog. P. putida binding lacks the increasing-affinity length trend reported for P. aeruginosa. Azotobacter chemistry remains homolog-based. Native AlgX also contributes to polymer protection/export, but this module represents its modification role.

PMID:25165982
P. aeruginosa AlgX directly O-acetylates polymannuronate using a surrogate donor.
PMID:23779107
Catalytic-site mutations abolish alginate acetylation in vivo; accessible primary abstract supports the mutation conclusion.
PMID:36494359
KT2440 AlgKX structure and polymer-binding experiments establish target-specific architecture and affinity behavior; Pa native interface disruption affects secretion/biofilm attachment.
PMID:10352233
Azotobacter algX is sequenced in the alginate locus; no direct target polymer-transfer assay is claimed.