Gene Ontology annotation through association of InterPro records with GO terms.

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

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

PMID:30351021

Lanmodulin: A Highly Selective Lanthanide-Binding Protein from a Lanthanide-Utilizing Bacterium.

LanM exhibits 100 million-fold selectivity for La(3+) over Ca(2+)

"whereas it only responds to CaII at near-millimolar concentrations"
Undergoes large conformational change from disordered to ordered state in response to picomolar concentrations of all LnIII

"LanM undergoes a large conformational change from a largely disordered state to a compact, ordered state in response to picomolar concentrations of all LnIII (Ln = La-Lu, Y)"
Contains four EF-hand motifs with unique proline residues that play key role in metal selectivity

"LanM possesses four metal-binding EF hand motifs... conserved proline residues present in LanM's EF hands, not encountered in CaII-binding EF hands... these unique proline residues play a key role in ensuring metal selectivity in vivo"

PMID:30352145

Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin.

NMR structure reveals unusual fusion of adjacent EF-hands resulting in compact fold unique among EF-hand proteins

"unusual fusion of adjacent EF-hands, resulting in a compact fold to the best of our knowledge unique among EF-hand-containing proteins"
Features unusual N i+1-H···N i hydrogen bonds involving unique EF-hand proline residues for selective LnIII recognition

"unusual N i+1-H···N i hydrogen bonds, in which LanM's unique EF-hand proline residues are engaged, in selective LnIII recognition"
Additional carboxylate ligand contributes to picomolar affinity for LnIIIs

"importance of an additional carboxylate ligand in contributing to the protein's picomolar affinity for LnIIIs"

PMID:32686425

Selective and Efficient Biomacromolecular Extraction of Rare-Earth Elements using Lanmodulin.

Most selective macromolecule for REEs characterized to date, outperforms many synthetic chelators

"LanM is the most selective macromolecule for REEs characterized to date and even outperforms many synthetic chelators"
Retains REE binding down to pH 2.5 and withstands temperatures up to 95°C

"LanM retains REE binding down to pH ≈ 2.5, and LanM-REE complexes withstand high temperature (up to 95 °C)"
Successfully applied to industrial feedstocks for quantitative and selective REE recovery

"After only a single all-aqueous step, quantitative and selective recovery of the REEs from all non-REEs initially present"

PMID:37259003

Enhanced rare-earth separation with a metal-sensitive lanmodulin dimer.

Demonstrates natural diversity of selective lanthanide recognition motifs across LanM family

"natural diversity of selective lanthanide recognition motifs"
X-ray crystal structures illustrate how picometre-scale differences in ionic radius are propagated to quaternary structure

"X-ray crystal structures illustrate how picometre-scale differences in radius between lanthanum(III) and dysprosium(III) are propagated to Hans-LanM's quaternary structure"

UniProt:C5B164

UniProt entry for lanmodulin

file:METEA/lanM/lanM-notes.md

Gene review notes for lanM

Part of rare earth element utilization machinery in methylotrophic bacteria
Lanthanides are essential cofactors for PQQ-dependent alcohol dehydrogenases in methylotrophs

file:METEA/lanM/lanM-deep-research-falcon.md

Falcon deep research report on lanM (lanmodulin, UniProt C5B164)

Primary molecular function is tight, high-affinity coordination of trivalent lanthanide ions; LanM acts as a macrochelator/chaperone-like mediator rather than an enzyme.

"its primary molecular function is **tight coordination of Ln3+ ions**"
LanM is not an enzyme but a high-affinity, high-selectivity lanthanide-binding macrochelator/mediator.

"(a “macrochelator”/chaperone-like mediator) rather than an enzyme"
LanM has four EF-hand motifs but only three (EF1-EF3) are high-affinity lanthanide-binding sites; EF4 has very low lanthanide affinity.

"only three sites (EF1–EF3) are high-affinity Ln-binding sites"
A conserved proline in the EF-hand loops supports strong lanthanide binding while diminishing calcium responsiveness, underpinning Ln-over-Ca selectivity.

"proline at position 2 in AM1 LanM) proposed to support strong lanthanide binding and diminished Ca2+ responsiveness"
LanM shows roughly 10^8-fold preference for lanthanides/Y(III) over calcium and other competing divalent metals.

"showing ~**10^8-fold** preference for **Ln3+/Y3+ over Ca2+**"
Lanthanide affinity is picomolar whereas calcium affinity is millimolar, consistent with extreme selectivity.

"picomolar Ln3+ affinity** and much weaker affinity for Ca2+ (reported as **millimolar**"
LanM binds approximately three equivalents of lanthanide at its three high-affinity sites.

"binding ~**3 equivalents** of lanthanides at its three high-affinity sites"
Lanthanide association is nearly diffusion-limited, with a very large association rate constant driving the exceptional overall affinity.

"Ln association is **nearly diffusion-limited**"
LanM is widely described as a periplasmic lanthanide mediator, supported by signal-peptide prediction and localization in a methylobacterial homolog.

"LanM is widely described as a **periplasmic lanthanide mediator**"
The consensus model is that LanM functions in periplasmic lanthanide homeostasis, protection, and solubilization rather than as a strictly required cofactor-delivery step.

"argue for a **homeostasis/protection/solubilization role in the periplasm**"
Deletion of lanM does not necessarily cause a clear lanthanide-dependent growth defect, implying redundancy or condition-specific roles.

"deleting lanM did not necessarily cause a clear Ln-dependent growth defect"
lanM expression is lanthanide-responsive (induced by La3+), linking it to lanthanide-responsive regulatory networks.

"lanM expression is **La3+-responsive**"
In a homolog, ΔlanM cells exposed to La3+ show aggregation, membrane permeability, and periplasmic La deposition, indicating a role in keeping lanthanides soluble/managed in the periplasm.

"ΔlanM** strains exposed to La3+ show **aggregation**, **membrane impairment/permeability**, and evidence of **periplasmic La deposition**"
LanM participates in a broader periplasmic protein-protein lanthanide-trafficking network (e.g., interaction with the lanthanide chaperone LanD) rather than acting alone.

"supporting an emerging view that LanM participates in a broader **protein–protein trafficking network**"