Annotation inferences using phylogenetic trees

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

PMID:16030218

Characterization of a multigene-encoded sodium/hydrogen antiporter (sha) from Pseudomonas aeruginosa: its involvement in pathogenesis.

Disruption of PA1054 causes Na+ sensitivity and decreased Na+ efflux, and the cluster lacking PA1054 does not restore antiport in E. coli TO114.

"Disruption of PA1054 resulted in severe Na+ sensitivity during growth and decreased Na+ efflux activity."
The PA1054 mutant is attenuated in mouse infection models.

"In mice, the deletion mutant of PA1054 also exhibited an attenuated virulence in systemic, pulmonary, and urinary tract infections"

PMID:20509166

A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli--expression and characterization of cytochrome-tagged Complex I subunits.

Cytochrome-tagged B. subtilis MrpA complements the Na+ sensitivity of a B. subtilis mrpA deletion strain (the experimental basis of the second seed of PTN000511949).

"The MrpA and MrpD antiporters remained functional after being fused to the cytochrome c-tag."

PMID:21236240

Homologous protein subunits from Escherichia coli NADH:quinone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis.

MrpA is proposed to carry Na+ and MrpD H+, together giving antiport.

"Presumably, MrpA transports Na+ whereas MrpD transports H+ in opposite directions, resulting in antiporter activity."

PMID:20624916

Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation.

Mrp antiport requires the hetero-oligomeric complex of all Mrp subunits.

"Antiport activity requires hetero-oligomeric complexes of all six or seven hydrophobic Mrp proteins (MrpA-MrpG)."

PMID:29218041

Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.

No Mrp antiporter shows antiport with MrpA or MrpD alone.

"In previous studies, none of the Mrp antiporters exhibited antiport activity with MrpA or MrpD alone."
In P. aeruginosa and V. cholerae, mrpA is fused with mrpB.

"in which it appears that the mrpA gene is fused with the mrpB gene encoding a fusion protein"

PMID:36241630

Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.

MrpA contains a proton transfer path through a histidine switch.

"His248MrpA accepts the proton from Lys353MrpA and delivers it to the conserved Lys/Glu pair of the MrpA subunit"

PMID:29754813

Structure of an Ancient Respiratory System.

Archaeal MBH has homologues of all Mrp subunits except MrpA.

"As noted above, MrpA is the only Mrp subunit that does not have a homolog in MBH"

file:PSEAE/PA1054/PA1054-uniprot.txt

UniProt entry Q9I4S0 (Q9I4S0_PSEAE)

file:PSEAE/PA1054/PA1054-bioinformatics/RESULTS.md

Composition of PAINT node PTN000511949 (PTHR43373) and its leaf IBAs