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biopolymer transporter ExbD
This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria [1]. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins [2]. [1]. 9371459. Unusual structure of the tonB-exb DNA region of Xanthomonas. campestris pv. campestris: tonB, exbB, and exbD1 are essential. for ferric iron uptake, but exbD2 is not.. Wiggerich HG, Klauke B, Koplin R, Priefer UB, Puhler A;. J Bacteriol 1997;179:7103-7110.. [2]. 3294803. Nucleotide sequence of a gene cluster involved in entry of E. colicins and single-stranded DNA of infecting filamentous. bacteriophages into Escherichia coli.. Sun TP, Webster RE;. J Bacteriol 1987;169:2667-2674. (from Pfam)
TonB system transport protein ExbD
TonB system transport protein ExbD is involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates
protein TolR
The model describes the inner membrane protein TolR, part of the TolR/TolQ complex that transduces energy from the proton-motive force, through TolA, to an outer membrane complex made up of TolB and Pal (peptidoglycan-associated lipoprotein). The complex is required to maintain outer membrane integrity, and defects may cause a defect in the import of some organic compounds in addition to the resulting morphologic. While several gene pairs homologous to talR and tolQ may be found in a single genome, but the scope of this model is set to favor finding only bone fide TolR, supported by operon structure as well as by score.
Members of this family are Gram-negative bacterial inner membrane proteins, generally designated ExbD, related to the TolR family modeled by TIGRFAMs TIGR02801. Members always are encoded next to a protein designated ExbB (TIGR02797), related to the TolQ family modeled by TIGRFAMs TIGR02796. ExbD and ExbB together form a proton channel through which they can harness the proton-motive force to energize TonB, which in turn energizes TonB-dependent receptors in the outer membrane. TonB-dependent receptors with known specificity tend to import siderophores or vitamin B12. A TonB system and Tol-Pal system often will co-exist in a single bacterial genome.
Membrane spanning protein in TonB-ExbB-ExbD complex; involved in the tonB-independent energy-dependent transport iron-siderophore complexes and vitamin B12 into the cell
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