Protein Family Models

This family locates between the N-terminal domain and MMR_HSR1 50S ribosome-binding GTPase of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This region is unknown for its function. (from Pfam)

Date:

2024-08-14

This entry represents the C-terminal domain of the HflX protein [1]. HflX binds to the intersubunit face of the 50S subunit. Its C-terminal domain (CTD) predominantly interacts with the NTD of uL11 at the bL12 stalk base. Truncation of the CTD rendered HflX inactive in 70S splitting [1]. Paper describing PDB structure 5ady. [1]. 26458047. HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions. Zhang Y, Mandava CS, Cao W, Li X, Zhang D, Li N, Zhang Y, Zhang X, Qin Y, Mi K, Lei J, Sanyal S, Gao N;. Nat Struct Mol Biol. 2015;22:906-913. (from Pfam)

Date:

2024-10-16

This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein. [1]. 19109926. E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides. Jain N, Dhimole N, Khan AR, De D, Tomar SK, Sajish M, Dutta D, Parrack P, Prakash B;. Biochem Biophys Res Commun. 2009;379:201-205. [2]. 19181811. Properties of HflX, an enigmatic protein from Escherichia coli. Dutta D, Bandyopadhyay K, Datta AB, Sardesai AA, Parrack P;. J Bacteriol. 2009;191:2307-2314. [3]. 19824612. Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach. Shields MJ, Fischer JJ, Wieden HJ;. Biochemistry. 2009;48:10793-10802. (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

GTPase HflX is a GTP-binding protein with a GTP hydrolysis activity that is stimulated by binding to the 50S ribosome subunit; it may play a role during protein synthesis or ribosome biogenesis

Date:

2017-02-03

This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like).

Gene:

hflX

Date:

2024-07-08

Involved in modulation of proteins HflK and HflC; part of the hflA locus (high frequency of lysogenization) which governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII protein

Gene:

hflX

Date:

2023-07-18