General description: Members of ECF287 are present in Actinobacteria (100%) and contain a conserved ~80 aa C-terminal extension of an unknown domain.
Anti-σ factor: No putative AS factor was found in the genetic context of members of ECF287.
Genomic context conservation: Members of ECF287 are encoded with transcriptional regulators from MerR family (0.44 and 0.22 per ECF of ECF287s1 and ECF287s2, respectively) and TetR family (0.22 and 0.57 per ECF of ECF287s1 and ECF287s2, respectively). Other conserved proteins in the genetic context of members of ECF287 include a soluble alpha/beta hydrolase encoded in position -1.
Summary: Members of ECF287 could be regulated by their C-terminal extension since they do not contain putative AS factors in their genetic context. The regulation could be carried out by disulfide bridges since the ECFs from ECF287 contain several conserved cysteine residues, also within their C-termini. A similar mechanism controls the activity 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: 57
Number of non-redundant ECFs: 55
Sequences with C-terminal extension: 98.18%
Sequences with N-terminal extension: 1.82%
Overrepresented order: Corynebacteriales [91.23%]
|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|