Gene Ontology annotation through association of InterPro records with GO terms

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

GO_REF:0000108

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

PMID:16030218

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

The PA1054-PA1059 cluster encodes a Na+/H+ antiporter; the abstract reports mutation of PA1054 only.

"We disrupted PA1054 (a shaA homologue gene) and determined its effect on Na+ tolerance during growth, Na+ efflux, and pathogenicity in mice."

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 MrpD complements a B. subtilis mrpD deletion strain (basis of the B. subtilis seed of PTN001865541).

"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.

B. subtilis mrpD deletion is Na+ and pH sensitive; MrpD is proposed to carry H+.

"Deletion of either mrpA or mrpD from the Bacillus subtilis chromosome resulted in a Na+ and pH sensitive growth phenotype."

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.

MrpD is needed for Mrp complex formation.

"These results suggested that the MrpD subunit is important in the formation of the Bp–Mrp complex."
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."

PMID:36241630

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

Proton binding at the MrpD Lys/Glu pair is proposed to drive Na+ transfer.

"Binding of the first proton to the Lys/Glu pair of MrpD drives the transfer of sodium bound at SLS1"

file:PSEAE/PA1056/PA1056-uniprot.txt

UniProt entry Q9I4R8 (Q9I4R8_PSEAE)

file:PSEAE/PA1056/PA1056-bioinformatics/RESULTS.md

Composition of PAINT node PTN001865541 (PTHR42703) and its leaf IBAs