Protein Family Models

Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains. (from Pfam)

Date:

2024-08-14

This domain is a helix-turn-helix domain that probably binds to DNA. (from Pfam)

Date:

2024-08-14

This family includes short-chain fatty acid regulators such as RAMB (regulator of acetate metabolism B), PCCR (Propionyl-CoA carboxylase regulator), PrpR (Propionate regulator). RamB is a negative transcriptional regulator of genes involved in acetate metabolism of C. glutamicum. It is responsible for expression control of the AK, PTA, ICL, and MS genes and, thus, for the proper adaptation to acetate as carbon and energy source. Nucleotide sequence analysis indicate the RamB protein consists of 469 aa with a putative HTH motif at the N terminus [1]. PCCR prevents the accumulation of propionyl-CoA by controlling expression of the gene encoding propionyl-CoA carboxylase, which is responsible for propionyl-CoA consumption by Rhodobacter sphaeroides. Many other Proteobacteria and Actinomycetales contain one or several PccR homologs that group into distinct clades on the basis of the pathway of acyl-CoA metabolism that they control [2]. PrpR is a transcriptional activator controlling prpDBC2 operon which encodes enzymes 2-methylcitrate dehydratase (PrpD2), 2-methylisocitrate lyase (PrpB2) and 2-methylcitrate synthase (PrpC2). They are essential for growth with propionate as carbon source. The regulatory protein belongs to the HTH_XRE regulator family. It has a length of 441 amino acids and an N-terminal lamda repressor-like DNA-binding domain [3]. [1]. 15090522. RamB, a novel transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum. Gerstmeir R, Cramer A, Dangel P, Schaffer S, Eikmanns BJ;. J Bacteriol. 2004;186:2798-2809. [2]. 26170412. Transcriptional Regulation by the Short-Chain Fatty . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR [2]. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae [1], HTH-type transcriptional regulators RamB [3] and PrpC [4]. [1]. 19150362. Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae. Vujicic-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, Sommer S, de Groot A, Serre L;. J Mol Biol. 2009;386:704-716. [2]. 18761623. A conserved anti-repressor controls horizontal gene transfer by proteolysis. Bose B, Auchtung JM, Lee CA, Grossman AD;. Mol Microbiol. 2008;70:570-582. [3]. 15090522. RamB, a novel transcriptional regulator of genes involved in acetate me. 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