General description: ECF21 has homology to original ECF21 (62.35%). Proteins in the base of ECF21s clade are present in Bacteroidetes (99.62%). Subgroups ECF21s12 and ECF21s29 are fused to the putative AS factors with an outer membrane beta-barrel, which are encoded in +1 for the rest of the subgroups.
Anti-σ factor: Members of ECF21 are mainly regulated by AS factors with one inner membrane transmembrane helix (71.31%) located in position +1 (except ECF21s12). These putative AS factors contain an outer-membrane beta-barrel in most of the cases, although, in some subgroups ECF21s9, ECF21s16, and ECF21s28, the AS factor and the outer membrane beta-barrel are decoupled and located in different proteins encoded in +1 and +2, respectively.
Genomic context conservation: The conservation of the genetic neighborhood is extensive in some subgroups and involves a protein from the radical SAM superfamily (ECF21s35 and +1 of ECF21s12), an oxidoreductase (ECF21s28, +2 of ECF21s12), a DUF4840 (-1 of ECF21s10), a polyprenyl synthetase (ECF21s1 and -1 of ECF21s26), a DNA primase (+3 of ECF21s26), a response regulator with a LuxR repressor (ECF21s1 and +4 of ECF21s26), a NAD synthase (ECF21s1 and +5 of ECF21s26), a RecA protein (-1 of ECF21s3 and ECF21s6), a FKBP-type peptidyl-prolyl cis-trans isomerase (+2 of ECF21s35), an adenylosuccinate lyase (ECF21s28), a thiolase (ECF21s13), two fumarase C (ECF21s16), a coenzyme A transferase (ECF21s6 and ECF21s3), a thioesterase (ECF21s3), a rhodanase (ECF21s3), an acyltransferase (ECF21s3), a GldH lipoprotein (ECF21s3), a haloacid dehalogenase (ECF21s32), a M42 glutamyl aminopeptidase (ECF21s35), an uracil phosphoribosyltransferase (ECF21s35), a phosphoribosyl transferase (ECF21s35) and a sodium/calcium exchanger (ECF21s35).
Summary: ECF21 might be regulated by AS factors encoded in +1. These AS factors contain one transmembrane helix and, in some cases, are fused to an outer membrane beta-barrel. In other instances, the outer membrane beta-barrel is encoded in the +2. No members of ECF21 have been functionally addressed.
Number of representative ECFs: 2391
Number of non-redundant ECFs: 2473
Sequences with C-terminal extension: 3.60%
Sequences with N-terminal extension: 0.77%
Overrepresented phylum: Bacteroidetes [99.75%]
|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|
|The extracytoplasmic function sigma factor EcfO protects Bacteroides fragilis against oxidative stress.||Journal of bacteriology||2012||I. Ndamukong, J. Gee, C. Smith||PubMed: 23104808||ECF21|
|Design of orthogonal genetic switches based on a crosstalk map of σs, anti-σs, and promoters.||Molecular systems biology||2013||V. Rhodius, T. Segall-Shapiro, B. Sharon, A. Ghodasara, E. Orlova, H. Tabakh, D. Burkhardt, K. Clancy, T. Peterson, C. Gross, C. Voigt||PubMed: 24169405||ECF22, ECF27, ECF03, ECF21, ECF39, ECF25, ECF26, ECF42, ECF38, ECF14, ECF29, ECF33, ECF281, ECF290, ECF291|