algE

UniProt ID: Q88NC8
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
πŸ“ Provide Detailed Feedback

Gene Description

AlgE is the predicted outer-membrane alginate export channel of Pseudomonas putida KT2440. Specific family identity and experimentally characterized Pseudomonas aeruginosa orthologs support a beta-barrel pore that provides a route for polymer secretion. A modeled KT2440 AlgEKX arrangement links it to the periplasmic AlgK–AlgX complex, but that complete assembly and native target polymer transport have not been experimentally established.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0009279 cell outer membrane
IEA
GO_REF:0000044
ACCEPT
Summary: AlgE is an outer-membrane protein.
Reason: The curated target compartment and specific channel family plus ortholog structure support localization. A predicted KT2440 AlgEKX model is not a direct localization assay.
Supporting Evidence:
file:PSEPK/algE/algE-deep-research-falcon.md
AlgE is an **outer-membrane (OM) Ξ²-barrel porin** that forms the **outer-membrane channel for alginate export**
file:PSEPK/algE/algE-uniprot.txt
SUBCELLULAR LOCATION: Cell outer membrane
PMID:21778407
monomeric 18-stranded Ξ²-barrel
GO:0042121 alginic acid biosynthetic process
IEA
GO_REF:0000041
ACCEPT
Summary: AlgE contributes the outer-membrane polymer export route.
Reason: Family-supported pore function and Pa channel/loop-mutant evidence support machinery participation in alginate production; polymer synthesis is performed by Alg8, not AlgE.
Supporting Evidence:
file:PSEPK/algE/algE-uniprot.txt
Belongs to the AlgE family.
file:PSEPK/algE/algE-uniprot.txt
Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore
PMID:21778407
monomeric 18-stranded Ξ²-barrel
GO:0015159 polysaccharide transmembrane transporter activity
ISS
PMID:21778407
Structural basis for alginate secretion across the bacterial...
NEW
Summary: AlgE-family identity supports inferred polysaccharide transport across the outer membrane.
Reason: GO:0015159 explicitly describes transfer of a polysaccharide across a membrane and therefore includes alginate. The target curated probable alginate-pore function, specific AlgE family and Pa structure/flux/loop-mutant evidence support an ISS proposal. Neither existing row is a molecular function, and no existing or replacement MF duplicates this claim. Native KT2440 polymer-translocation measurements are not asserted. A separate alginate-channel NTR is not required to distinguish this activity from ion transport.
Supporting Evidence:
file:PSEPK/algE/algE-uniprot.txt
Belongs to the AlgE family.
file:PSEPK/algE/algE-uniprot.txt
Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore
PMID:21778407
monomeric 18-stranded Ξ²-barrel

Core Functions

Inferred outer-membrane alginate export channel. Specific family identity and ortholog structure, anion flux and native mutant phenotypes support this route; direct polymer tracking through the target pore remains untested.

Supporting Evidence:
  • file:PSEPK/algE/algE-uniprot.txt
    Belongs to the AlgE family.
  • file:PSEPK/algE/algE-uniprot.txt
    Has non-porin-like, channel-forming properties and probably functions as an alginate permeability pore
  • PMID:21778407
    monomeric 18-stranded Ξ²-barrel

References

Loading supporting content…

Download this section (compressed HTML)

Suggested Questions for Experts

Q: Does KT2440 AlgE form an alginate-specific outer-membrane pore with substrate selectivity comparable to characterized AlgE homologs?

Suggested Experiments

Experiment: Reconstitute AlgE in proteoliposomes or planar bilayers and test alginate-dependent channel conductance and polymer passage.

Type: membrane channel assay

Deep Research

Falcon

(algE-deep-research-falcon.md)

Loading supporting content…

Download this section (compressed HTML)

πŸ“š Additional Documentation

Notes

(algE-notes.md)

Loading supporting content…

Download this section (compressed HTML)

πŸ“„ View Raw YAML

Loading supporting content…

Download this section (compressed HTML)