P0AFX7 · RSEA_ECOLI
- ProteinAnti-sigma-E factor RseA
- GenerseA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids216 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E. Overexpression of RseA blocks sigma-E from acting, results in cell lysis in stationary phase and temperature-sensitivity above 37 degrees Celsius.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 108-109 | Cleavage; by RseP | ||||
Sequence: AC | ||||||
Site | 148-149 | Cleavage; by DegS | ||||
Sequence: VS |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | sigma factor antagonist complex | |
Molecular Function | molecular adaptor activity | |
Molecular Function | sigma factor antagonist activity | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | response to stress |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnti-sigma-E factor RseA
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AFX7
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Single-pass type II membrane protein
Note: Following cleavage by DegS the large fragment of the protein is still in the inner membrane and retains its anti-sigma-E activity.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-100 | Cytoplasmic | ||||
Sequence: MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQ | ||||||
Transmembrane | 101-118 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LTQMGVAACVSLAVIVGV | ||||||
Topological domain | 119-216 | Periplasmic | ||||
Sequence: QHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
About 10-fold increased sigma-E activity. Neither sigma-E nor RseB associate with the inner membrane.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1-28 | Loss of anti-sigma factor activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 11 | Loss of anti-sigma factor activity. | ||||
Sequence: D → H | ||||||
Mutagenesis | 19 | Loss of anti-sigma factor activity. | ||||
Sequence: L → P | ||||||
Mutagenesis | 33 | Loss of anti-sigma factor activity. | ||||
Sequence: W → C | ||||||
Mutagenesis | 79 | No binding of N-terminal fragment to SspB. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 85 | No binding of N-terminal fragment to SspB. | ||||
Sequence: W → A | ||||||
Mutagenesis | 88 | Reduced binding of N-terminal fragment to SspB. | ||||
Sequence: M → A | ||||||
Mutagenesis | 107-108 | Significantly less degradation by ClpX-ClpP when present as a 1-108 peptide fragment. | ||||
Sequence: AA → DD | ||||||
Mutagenesis | 146 | No effect on protein cleavage. | ||||
Sequence: S → X | ||||||
Mutagenesis | 147 | No effect on protein cleavage in vitro and in vivo. | ||||
Sequence: P → X | ||||||
Mutagenesis | 148 | Normal cleavage by DegS and RseP in vitro (PubMed:19706448), for A-148 decreased cleavage by DegS in vivo (PubMed:23016873). | ||||
Sequence: V → A, C, I, L, M, N, or T | ||||||
Mutagenesis | 148 | Not cleaved by DegS nor RseP in vitro (PubMed:19706448). | ||||
Sequence: V → D, E, G, F, or P | ||||||
Mutagenesis | 148 | Cleaved by DegS but not by RseP in vitro (PubMed:19706448), for R-148 and S-148 decreased cleavage by DegS in vivo (PubMed:23016873). | ||||
Sequence: V → H, K, Q, R, S, or Y | ||||||
Mutagenesis | 162-169 | RseA is degraded by RseP in the absence of DegS. | ||||
Sequence: QQQQVQEQ → AAAAVAEA | ||||||
Mutagenesis | 172 | Still binds RseB. No binding to RseB; when associated with A-185. | ||||
Sequence: R → A | ||||||
Mutagenesis | 172 | No binding to RseB. | ||||
Sequence: R → D | ||||||
Mutagenesis | 185 | Still binds RseB. No binding to RseB; when associated with A-172. | ||||
Sequence: R → A | ||||||
Mutagenesis | 185 | No binding to RseB. | ||||
Sequence: R → E | ||||||
Mutagenesis | 190-200 | RseA is degraded by RseP in the absence of DegS. | ||||
Sequence: QLQFEQAQTQQ → ALAFFAAATAA |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097480 | 1-216 | Anti-sigma-E factor RseA | |||
Sequence: MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ |
Post-translational modification
Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2 protease) between positions Ala-108 and Cys-109. The N-terminal fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE from RseA.
Proteomic databases
Interaction
Subunit
Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this inhibits the interaction of sigma-E with the RNA polymerase catalytic core and leads to a decreased expression of sigma-E-regulated genes. Interacts with RseB with 1:1 stoichiometry. The liberated N-terminus (residues 1-108) forms a complex with SspB and RpoE; binding to SspB is competitively inhibited by ssrA-tags, although the 2 proteins bind in opposite directions in SspB's peptide-binding groove.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0AFX7 | degS P0AEE3 | 7 | EBI-1117560, EBI-1132101 | |
BINARY | P0AFX7 | rseB P0AFX9 | 9 | EBI-1117560, EBI-1135231 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-97 | Sufficient to repress sigma-E | ||||
Sequence: MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPW | ||||||
Region | 146-166 | Disordered | ||||
Sequence: SPVSLGVPSEATANNGQQQQV | ||||||
Compositional bias | 152-166 | Polar residues | ||||
Sequence: VPSEATANNGQQQQV | ||||||
Coiled coil | 158-202 | |||||
Sequence: ANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAA | ||||||
Region | 169-186 | Primary binding site for RseB | ||||
Sequence: QRRRINAMLQDYELQRRL | ||||||
Region | 190-200 | Poly-Gln (Q2) | ||||
Sequence: QLQFEQAQTQQ |
Domain
The N-terminal cytosolic domain interacts with sigma-E, and upon overexpression leads to temperature sensitivity above 37 degrees Celsius and cell lysis in stationary phase. After degradation by RseP residues 77-108 bind to SspB, targeting RseA for degradation by the ClpX-ClpP protease.
The C-terminal periplasmic domain (residues 169-186) interacts with RseB and is also the target for DegS; RseB and DegS binding sites do not appreciably overlap. Gln-rich regions (residues 162-169, Q1, and 190-200, Q2) contribute to preventing RseP from acting before DegS. Insertion of 8 consecutive Gln residues into a protein lacking Q1 and Q2 restores DegS-dependence of RseP cleavage.
Sequence similarities
Belongs to the RseA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length216
- Mass (Da)24,321
- Last updated2005-12-20 v1
- Checksum63BD12131C611C32
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 152-166 | Polar residues | ||||
Sequence: VPSEATANNGQQQQV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10148 EMBL· GenBank· DDBJ | AAA83999.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U37089 EMBL· GenBank· DDBJ | AAC45315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D64044 EMBL· GenBank· DDBJ | BAA10919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D13169 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U00096 EMBL· GenBank· DDBJ | AAC75625.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76748.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U37455 EMBL· GenBank· DDBJ | AAC45318.1 EMBL· GenBank· DDBJ | Genomic DNA |