Protein Family Models

helix-turn-helix domain-containing protein such as an XRE (Xenobiotic Response Element) family transcriptional regulator

Date:

2024-04-02

This domain is found at the C-terminal end of HTH-type transcriptional regulator Rgg from Streptococcus gordonii, and similar proteins predominantly found in Firmicutes. Rgg is a peptide pheromone receptor that directly binds pheromones transported to the cytosol. The large C-terminal repeat domain contains five HTH folds and a capping helix that form a right-handed superhelical structure, resembling a TPR domain superhelix [1-5]. This domain is found associated with the N-terminal Pfam:PF01381. Paper describing PDB structure 2aw6. [1]. 16339309. Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis. Shi K, Brown CK, Gu ZY, Kozlowicz BK, Dunny GM, Ohlendorf DH, Earhart CA;. Proc Natl Acad Sci U S A. 2005;102:18596-18601. Paper describing PDB structure 2grm. [2]. 17038121. Molecular basis for control of conjugation by bacterial pheromone and inhibitor peptides. Kozlowicz BK, Shi K, Gu ZY, Ohlendorf DH, Earhart CA, Dunny GM;. Mol Microbiol. 2006;62:958-969. Paper describing PDB structure 4yv6. [3]. 25847993. Rgg protein structure-function and inhibition by cyclic peptide compounds. Parashar V, Aggarwal C, Federle MJ, Neiditch MB;. Proc Natl Acad Sci U S A. 2015;112:5177-5182. Paper describing PDB structure 5dl2. [4]. 26714274. Structural and functional analysis of RopB: a major virulence regulator in Streptococcus pyogenes. Makthal N, Gavagan M, Do H, Olsen RJ, Musser JM, Kumaraswami M;. Mol Microbiol. 2016;99:1119-1133. Paper describing PDB structure 5w4m. [5]. 29030429. Activating mutations in quorum-sensing regulator Rgg2 and its conformational. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This large family of DNA binding helix-turn helix proteins includes Cro Swiss:P03036 and CI Swiss:P03034. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family [1]. [1]. 20196080. The crystal structure of NGO0477 from Neisseria gonorrhoeae reveals a novel protein fold incorporating a helix-turn-helix motif. Ren J, Sainsbury S, Nettleship JE, Saunders NJ, Owens RJ;. Proteins. 2010;78:1798-1802. (from Pfam)

Date:

2024-10-16

This HMM describes the whole, except for a 60 residue N-terminal helix-turn-helix DNA-binding domain (PFAM PF01381) of the family of proteins related to the transcriptional regulator Rgg, also called RopB. Rgg is required for secretion of several proteins, including a cysteine proteinase associated with virulence. GadR (GP|2352485) is a positive regulator of a glutamate-dependent acid resistance mechanism. MutR is a transcriptional activator for mutacin biosynthesis genes in Streptococcus mutans. This family appears restricted to the low-GC Gram-positive bacteria, including at least eight members in Lactococcus lactis.

Date:

2021-05-12