General description: Members of ECF288 appear in Firmicutes (100%) and contain a C-terminal extension of ~100 amino acids. Interestingly, both σ4 domain and the C-terminal extension of members of ECF288 contain multiple cysteine residues, which indicates that disulfide-bridge formation could be in charge of the modulation of their activity, as in the case of SigK from M. tuberculosis (Shukla et al., 2014) (ECF19s2) and CorE2 from M. xanthus (Marcos-Torres et al., 2016; Torres et al., 2018) (ECF238s15).
Anti-σ factor: No putative AS factors were found in the genetic context of members of ECF288. Nevertheless, there is a soluble conserved DUF2461-containing protein in +1, which might be part of the regulatory mechanism of ECF288.
Promoter motif conservation: Predicted target promoter motifs are highly conserved, with TGTCACA in -35 and TGTCTAAT in -10.
Summary: In conclusion, proteins ECF288 contains C-rich C-terminal extensions that could be in charge of their activation or inactivation as in the case of CorE2 from M. xanthus (Marcos-Torres et al., 2016; Torres et al., 2018) (ECF238s15) and SigK from M. tuberculosis (Shukla et al., 2014) (ECF19s2).
Number of representative ECFs: 73
Number of non-redundant ECFs: 74
Sequences with C-terminal extension: 100.00%
Sequences with N-terminal extension: 0.00%
Overrepresented class: Clostridia [76.71%]
|Structural basis for the redox sensitivity of the Mycobacterium tuberculosis SigK-RskA σ-anti-σ complex.||Acta crystallographica. Section D, Biological crystallography||2014||J. Shukla, R. Gupta, K. Thakur, R. Gokhale, B. Gopal||PubMed: 24699647||ECF57, ECF19, ECF18, ECF288|
|In depth analysis of the mechanism of action of metal-dependent sigma factors: characterization of CorE2 from Myxococcus xanthus.||Nucleic acids research||2016||F. Marcos-Torres, J. Pérez, N. Gómez-Santos, A. Moraleda-Muñoz, J. Muñoz-Dorado||PubMed: 26951374||ECF238, ECF287, ECF288|
|The complex global response to copper in the multicellular bacterium Myxococcus xanthus.||Metallomics : integrated biometal science||2018||J. Pérez, J. Muñoz-Dorado, A. Moraleda-Muñoz||PubMed: 29961779||ECF238, ECF287, ECF288|