Protein Family Models

FeoB is a G-protein coupled membrane protein essential for Fe(II) uptake in prokaryotes. In the structures, a canonical G-protein domain (G domain) is followed by a helical bundle domain (S-domain) which is represented by this entry. [1]. 20123128. Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB. Hung KW, Chang YW, Eng ET, Chen JH, Chen YC, Sun YJ, Hsiao CD, Dong G, Spasov KA, Unger VM, Huang TH;. J Struct Biol. 2010;170:501-512. [2]. 19629046. Structural basis of GDP release and gating in G protein coupled Fe2+ transport. Guilfoyle A, Maher MJ, Rapp M, Clarke R, Harrop S, Jormakka M;. EMBO J. 2009;28:2677-2685. [3]. 19733088. Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter. Hattori M, Jin Y, Nishimasu H, Tanaka Y, Mochizuki M, Uchiumi T, Ishitani R, Ito K, Nureki O;. Structure. 2009;17:1345-1355. [4]. 22101824. A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB. Ash MR, Maher MJ, Guss JM, Jormakka M;. Acta Crystallogr D Biol Crystallogr. 2011;67:973-980. [5]. 20220129. Potassium-activated GTPase reaction in the G Protein-coupled ferrous iron transporter B. Ash MR, Guilfoyle A, Clarke RJ, Guss JM, Maher MJ, Jormakka M;. J Biol Chem. 2010;285:14594-14602. [6]. 21858085. The initiation of GTP hydrolysis by the G-domain of FeoB: insights from a transition-state complex structure. Ash MR, Maher MJ, Guss JM, Jormakka M;. PLoS One. 2011;6:e23355. [7]. 22139154. The structure of an N11A mutant of the G-protein domain of FeoB. Ash MR, Maher MJ, Guss JM, Jormakka M;. Acta Crys. TRUNCATED at 1650 bytes (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 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

This family includes FeoA a small protein, probably involved in Fe2+ transport [1]. This presumed short domain is also found at the C-terminus of a variety of metal dependent transcriptional regulators. This suggests that this domain may be metal-binding. In most cases this is likely to be either iron or manganese. [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

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

FeoA and FeoB domain-containing protein

Date:

2017-03-02

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

Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once. This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.

Date:

2022-03-28