P40685 · CHRR_CERS4
- ProteinAnti-sigma-E factor ChrR
- GenechrR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids213 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulating the transcription of the cycA and rpoE genes. ECF sigma factors are held in an inactive form by a cognate anti-sigma factor.
Cofactor
Note: Binds 2 Zn2+ ion per subunit. The Zn2+ bound by the N-terminus is required for anti-sigma function, the function of the Zn2+ bound by the C-terminus is unknown.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 6 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 31 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 35 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 38 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 141 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 143 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 147 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 177 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAnti-sigma-E factor ChrR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Cereibacter
Accessions
- Primary accessionP40685
- Secondary accessions
Proteomes
Phenotypes & Variants
Disruption phenotype
For single chrR mutant about 12-fold increase in rpoE-regulated genes. For double rpoE-chrR deletion mutant no effect on anaerobic photosynthetic growth. In illuminated aerobically growing cells double deletion is bacteriostatic.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 5 | No effect on anti-sigma function. | |||
Mutagenesis | 6 | Loss of anti-sigma function. | |||
Mutagenesis | 31 | No effect on anti-sigma function. | |||
Mutagenesis | 35 | Loss of anti-sigma function. | |||
Mutagenesis | 35 | Loss of function; no effect on zinc binding. | |||
Mutagenesis | 38 | Loss of anti-sigma function. | |||
Mutagenesis | 38 | In Chr4 mutant; loss of function. | |||
Mutagenesis | 38 | Loss of ability to bind zinc. | |||
Mutagenesis | 187 | No effect on zinc binding. | |||
Mutagenesis | 189 | No effect on zinc binding. | |||
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Chain | PRO_0000089658 | 2-213 | Anti-sigma-E factor ChrR | ||
Expression
Induction
Induced by singlet oxygen. Autoregulated. Part of the rpoE-chrR operon.
Interaction
Subunit
Forms a 1:1 complex with cognate ECF RNA polymerase sigma factor RpoE; this inhibits the interaction of RpoE with the RNA polymerase catalytic core.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 2-85 | Sufficient to bind sigma factor and inhibit its activity | |||
Region | 86-194 | Required for response to singlet oxygen | |||
Domain
The N-terminal anti-sigma domain (residues 1-85) is necessary and sufficient to bind sigma-E and inhibit its activity. The C-terminal domain (residues 86-194) is required to respond to singlet oxygen (PubMed:17803943).
Sequence similarities
Belongs to the zinc-associated anti-sigma factor (ZAS) superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length213
- Mass (Da)22,865
- Last updated2007-01-23 v4
- Checksum46152BC5858C845F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U11283 EMBL· GenBank· DDBJ | AAB17905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000143 EMBL· GenBank· DDBJ | ABA80279.1 EMBL· GenBank· DDBJ | Genomic DNA |