Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
TonB N-terminal domain-containing protein
TonB from Escherichia coli and its homologues are critical for the uptake of siderophores through the outer membrane of Gram-negative bacteria using chemiosmotic energy. The proline-rich segment of TonB exists in a PPII-like conformation [1]. The result implies that the proline-rich segment of TonB possesses a length of more than 15 nm, sufficient to span the periplasm of Gram-negative bacteria. [1]. 20095050. The proline-rich domain of TonB possesses an extended. polyproline II-like conformation of sufficient length to span. the periplasm of Gram-negative bacteria.. Kohler SD, Weber A, Howard SP, Welte W, Drescher M;. Protein Sci. 2010;19:625-630. (from Pfam)
energy transducer TonB
The TonB_C domain is the well-characterised C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane [1]. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance [2]. [1]. 16741124. Outer membrane active transport: structure of the BtuB:TonB. complex.. Shultis DD, Purdy MD, Banchs CN, Wiener MC;. Science. 2006;312:1396-1399.. [2]. 21277822. Recent insights into iron import by bacteria.. Braun V, Hantke K;. Curr Opin Chem Biol. 2011;15:328-334. (from Pfam)
energy transducer TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.)
TonB family protein
This HMM represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm.
TonB system transport protein TonB
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on