Regulation: Members of ECF265 are associated with AS factors with one transmembrane helix (51.87%) in +1. In the case of ECF265s4 and ECF265s7, which appear primarily in the Bacillus genus, there is no apparent AS factor in their genetic context. In these groups, ECFs share the genetic neighborhood with a transcriptional repressor from PadR family (+1) and a cell cycle protein (+2) involved in peptidoglycan synthesis such as FtsW, RodA or SpoVE (Pfam: PadR and FTSW_RODA_SPOVE) in +1 and +2, respectively. PadR is involved in negative regulation of the phenolic acid metabolism and RodA is a peptidoglycan glycosyltransferase involved in peptidoglycan biosynthesis. It is possible that in these two subgroups the AS factor is substituted by transcriptional control.
Genomic context conservation: Apart from the proteins mentioned above, the only conserved element in the genomic neighborhood of members of ECF265 are the inner-membrane component of an ABC transporter (Pfam: BPD_transp_1) (ECF265s24).
Promoter motif conservation: Promoter motifs are subgroup-dependent conserved and usually contain AAC in -35 and CGTC in -10; in agreement with the prediction for original ECF30 (Staroń et al., 2009).
Summary: In summary, ECF265 seems to be regulated by putative AS factors encoded in +1 with diverse unknown domains, in contrast to original ECF30 (Staroń & Mascher, 2010). Two subgroups, ECF265s4 and ECF265s7, seem to be regulated by a PadR transcriptional repressor encoded in +1 and involved in phenolic acid metabolism. Since RodA is encoded in position +2 in ECF265s4 and ECF265s7, proteins from these subgroups might be involved in peptidoglycan biosynthesis.
Number of representative ECFs: 1328
Number of non-redundant ECFs: 1781
Sequences with C-terminal extension: 0.11%
Sequences with N-terminal extension: 1.80%
Overrepresented phylum: Firmicutes [97.36%]
|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||ECF114, ECF31, ECF22, ECF12, ECF27, ECF122, ECF121, ECF56, ECF03, ECF21, ECF23, ECF02, ECF41, ECF15, ECF107, ECF111, ECF39, ECF19, ECF25, ECF17, ECF26, ECF118, ECF11, ECF16, ECF42, ECF38, ECF103, ECF36, ECF28, ECF51, ECF115, ECF40, ECF14, ECF29, ECF123, ECF33, ECF102, ECF105, ECF106, ECF116, ECF130, ECF18, ECF235, ECF120, ECF239, ECF240, ECF242, ECF243, ECF249, ECF265, ECF271, ECF281, ECF285, ECF286, ECF289, ECF290, ECF291, ECF292, ECF293, ECF294, ECF30, ECF32, ECF43|
|General stress response in α-proteobacteria: PhyR and beyond.||Molecular microbiology||2010||A. Staroń, T. Mascher||PubMed: 20979331||ECF265|