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Literature summary for 7.6.2.9 extracted from

  • Teichmann, L.; Kuemmel, H.; Warmbold, B.; Bremer, E.
    OpuF a new Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the trans-membrane domain (2018), Appl. Environ. Microbiol., 84, e01728-18 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.6.2.9

Cloned(Commentary)

Cloned (Comment) Organism
gene opuF, functional expression and resonstitution of the OpuF transporter in Bacillus subtilis Bacillus infantis
gene opuF, functional expression and resonstitution of the OpuF transporter in Bacillus subtilis Ectobacillus panaciterrae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the solute ABC transporter has a substrate-binding protein fused to the transmembrane domain Bacillus infantis 16020
-
membrane the solute ABC transporter has a substrate-binding protein fused to the transmembrane domain Ectobacillus panaciterrae 16020
-

Organism

Organism UniProt Comment Textmining
Bacillus infantis
-
-
-
Ectobacillus panaciterrae
-
-
-
no activity in Bacillus subtilis
-
 no activity of ABC transporter OpuF
-

Renatured (Commentary)

Renatured (Comment) Organism
functional expression and resonstitution of the OpuF transporter in Bacillus subtilis Bacillus infantis
functional expression and resonstitution of the OpuF transporter in Bacillus subtilis Ectobacillus panaciterrae

Synonyms

Synonyms Comment Organism
OpuF
-
 Bacillus infantis
OpuF
-
 Ectobacillus panaciterrae
OpuF transporter
-
 Bacillus infantis
OpuF transporter
-
 Ectobacillus panaciterrae

General Information

General Information Comment Organism
evolution OpuF is a member of the Opu family of transporters. OpuF is not present in Bacillus subtilis but it is widely distributed in members of the large Bacillus genus. OpuF is a representative of a sub-group of ABC transporters in which the substrate-binding protein (SBP) is fused to the trans-locating subunit (TMD). The OpuF system is a representative of a growing sub-group of ABC transporters in which the substrate-scavenging function of the SBP and the membrane-embedded substrate TMD are fused into a single polypeptide chain Bacillus infantis
evolution OpuF is a member of the Opu family of transporters. OpuF is widely distributed in members of the large Bacillus genus. OpuF is a representative of a sub-group of ABC transporters in which the substrate-binding protein (SBP) is fused to the trans-locating subunit (TMD). The OpuF system is a representative of a growing sub-group of ABC transporters in which the substrate-scavenging function of the SBP and the membrane-embedded substrate TMD are fused into a single polypeptide chain Ectobacillus panaciterrae
additional information an in silico model of the substrate-binding protein (SBP) domain of the transmembrane domain (TMD)-SPB hybrid protein OpuFB is established. It reveals the presence of an aromatic cage, a structural feature commonly present in ligand-binding sites of compatible solute importers Bacillus infantis
additional information an in silico model of the substrate-binding protein (SBP) domain of the transmembrane domain (TMD)-SPB hybrid protein OpuFB is established. It reveals the presence of an aromatic cage, a structural feature commonly present in ligand-binding sites of compatible solute importers Ectobacillus panaciterrae
physiological function OpuF is another Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the transmembrane domain. OpuF mediates the import of glycine betaine, proline betaine, homobetaine and the marine osmolyte dimethylsulfoniopropionate (DMSP). The high affinity import of compatible solutes from environmental sources is an important aspect of the cellular defense of many Bacteria and Archaea against the harmful effects of high external osmolarity. The accumulation of these osmostress protectants counteracts high osmolarity instigated water efflux, drop in turgor to non-physiological values, and an undue increase in molecular crowding of the cytoplasm, they thereby foster microbial growth under osmotically unfavorable conditions Bacillus infantis
physiological function OpuF is another Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the transmembrane domain. OpuF mediates the import of glycine betaine, proline betaine, homobetaine and the marine osmolyte dimethylsulfoniopropionate (DMSP). The high affinity import of compatible solutes from environmental sources is an important aspect of the cellular defense of many Bacteria and Archaea against the harmful effects of high external osmolarity. The accumulation of these osmostress protectants counteracts high osmolarity instigated water efflux, drop in turgor to non-physiological values, and an undue increase in molecular crowding of the cytoplasm, they thereby foster microbial growth under osmotically unfavorable conditions Ectobacillus panaciterrae