General description: Members of ECF115 are present in Firmicutes (100%) from order Bacillales and have homology to original group ECF115 (40.3%) (Staroń et al., 2009). Members of ECF115 contain a C-terminal extension with several possible domains. This C-terminal extension is typical of ~70aa long, although in subgroup ECF115s3, where the C-terminal extension contains a SnoaL-like domain (Pfam: SnoaL_2), it extends to up to ~130 aa.
Genomic context conservation: Members of ECF115 contain a Clp protease in their genetic context (except ECF115s3). Clp proteases are in charge of the last step of the degradation of AS factors regulated by RIP (Barchinger & Ades, 2013). Genetic context conservation is not conserved beyond the Clp protease.
Anti-σ factor: no putative AS factor is present in the genetic context of members of ECF115.
Promoter motif conservation: Predicted target promoter motifs contain ATC in -35 and CGT in -10.
Summary: Members of ECF115 could be regulated by their C-terminal extension and the Clp protease encoded in their genetic neighborhood. The protease could cleave the C-terminal extension, leaving the ECF free to bind the RNAP and its target promoter. Another possibility is that the Clp protease is the target of the regulation of ECF115. Interestingly, the only subgroup with a different C-terminal extension, ECF115s3 with a SnoaL-like domain, lacks the Clp protease, indicating that only ECF115-like C-termini need the presence of the protease.
Number of representative ECFs: 294
Number of non-redundant ECFs: 536
Sequences with C-terminal extension: 99.44%
Sequences with N-terminal extension: 0.56%
Overrepresented family: Bacillaceae [58.50%]
|The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) sigma factor protein family.||Molecular microbiology||2009||A. Staroń, H. Sofia, S. Dietrich, L. Ulrich, H. Liesegang, T. Mascher||PubMed: 19737356||ECF103, ECF21, ECF123, ECF51, ECF39, ECF281, ECF102, ECF130, ECF122, ECF291, ECF15, ECF242, ECF22, ECF285, ECF106, ECF27, ECF31, ECF240, ECF114, ECF16, ECF38, ECF41, ECF105, ECF116, ECF111, ECF03, ECF239, ECF42, ECF294, ECF17, ECF11, ECF29, ECF235, ECF293, ECF118, ECF265, ECF30, ECF23, ECF14, ECF249, ECF18, ECF115, ECF290, ECF25, ECF121, ECF02, ECF120, ECF289, ECF28, ECF243, ECF19, ECF43, ECF107, ECF12, ECF32, ECF36, ECF292, ECF286, ECF271, ECF26, ECF40, ECF56, ECF33|
|Regulated proteolysis: control of the Escherichia coli σ(E)-dependent cell envelope stress response.||Sub-cellular biochemistry||2013||S. Barchinger, S. Ades||PubMed: 23479440||ECF115|