Protein Family Models

Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions [1]. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N-terminus has been previously erroneously described as being ATP-binding [1]. Recent work shows that it is similar to eukaryotic G-proteins and that it is a GTPase [2]. [1]. 8407793. Characterization of the ferrous iron uptake system of Escherichia coli. Kammler M, Schon C, Hantke K;. J Bacteriol 1993;175:6212-6219. [2]. 12446835. The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM;. Proc Natl Acad Sci U S A 2002;99:16243-16248. (from Pfam)

Date:

2024-10-16

This region in the nucleoside transporter proteins are responsible for determining nucleoside specificity in the human CNT1 and CNT2 proteins (e.g Swiss:O00337) [1]. In the FeoB proteins (e.g. Swiss:O25396), which are believed to be Fe2+ transporters, it includes the membrane pore region, so the function of this region is likely to be more general than just nucleoside specificity [2]. This family may represent the pore and gate, with a wide potential range of specificity. Hence its name 'Gate'. [1]. 10455109. Identification of amino acid residues responsible for the pyrimidine and purine nucleoside specificities of human concentrative Na(+) nucleoside cotransporters hCNT1 and hCNT2. Loewen SK, Ng AM, Yao SY, Cass CE, Baldwin SA, Young JD;. J Biol Chem 1999;274:24475-24484. [2]. 12781516. Is the bacterial ferrous iron transporter FeoB a living fossil?. Hantke K;. Trends Microbiol 2003;11:192-195. (from Pfam)

Date:

2024-10-16

Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions [1]. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent [1]. [1]. 8407793. Characterization of the ferrous iron uptake system of Escherichia coli. Kammler M, Schon C, Hantke K;. J Bacteriol 1993;175:6212-6219. (from Pfam)

Date:

2024-10-16

This HMM identifies the P-loop-containing domain of large numbers of GTPases with ribosome-associated functions, including many involved in ribosome maturation (Der, Era, etc), ribosome rescue (HflX), and protein translation (InfB, Tuf, PrfC).

Date:

2024-10-16

FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum.

Gene:

feoB

Date:

2024-05-30